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Conserved domains on  [gi|2734168012|ref|WP_346412035|]
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porin [Serratia marcescens]

Protein Classification

porin( domain architecture ID 10007050)

porin forms an aqueous channel for the diffusion of small hydrophilic molecules across the outer membrane

CATH:  2.40.160.10
Gene Ontology:  GO:0009279|GO:0016020|GO:0015288
PubMed:  31214985|31792365
SCOP:  4003061
TCDB:  1.B.1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
OmpC COG3203
Outer membrane porin OmpC/OmpF/PhoE [Cell wall/membrane/envelope biogenesis];
9-365 3.71e-30

Outer membrane porin OmpC/OmpF/PhoE [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442436 [Multi-domain]  Cd Length: 336  Bit Score: 118.18  E-value: 3.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012   9 FIGGVLLSALSAGAQAeitildknpQSNVllaplslKVGGSIRPEWIFSNGPEPGYDK--NGHDGGTRFRFSGDYALTQD 86
Cdd:COG3203     2 LLALAVAAALAGAAHA---------QSSV-------TLYGRVDAGVEYVDNGGGSLTRltSGGDSGSRLGFKGSEDLGGG 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012  87 TSIIGYYEWGVDLAHALSwdghynEDGKRDYQRQLYAGFKDDRYGTLTYGHQYGIYYSVVGiksdVWDNDGHAGGTGIGI 166
Cdd:COG3203    66 LKAIFQLESGFNADTGTS------GGGGRLFGRQAYVGLKGDDFGTLTLGRQYTPLYDVVG----AFDPFGDSGDAGNLA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 167 SGD-YDGGNKPKNSIKYTN-DFGPVTLYANYLLPEDDLHTADNliyrrkGGGGLGFDYKvTKDFTFSAAYSYTDakiKDN 244
Cdd:COG3203   136 GDDnLAGTGRADNAIKYRSpNFGGLTFGAQYSFGEDAGSSSNG------RGYGAGLTYA-NGPLSLGAAYQQSN---DAQ 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 245 LYSEKDYHQQLSGTALTWQPNNWYIVGTASYYKDYVPSTrqrtlshFFAGDGYGLEGFVGYTFNidkPFLKSIQPYVAAD 324
Cdd:COG3203   206 GATAGGDDADAWGLGASYDFGNLKLAAGYGQTKNDDAGG-------AGNAKADGYELGASYPFG---PALTLSASYGYTD 275
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2734168012 325 SLRLKGDeaYHANHVYLGAGTTIGYGLSVYVERTLANSSDN 365
Cdd:COG3203   276 AKDGADD--DDANQYALGADYALSKRTSLYAEYGYNDNDGN 314
 
Name Accession Description Interval E-value
OmpC COG3203
Outer membrane porin OmpC/OmpF/PhoE [Cell wall/membrane/envelope biogenesis];
9-365 3.71e-30

Outer membrane porin OmpC/OmpF/PhoE [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442436 [Multi-domain]  Cd Length: 336  Bit Score: 118.18  E-value: 3.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012   9 FIGGVLLSALSAGAQAeitildknpQSNVllaplslKVGGSIRPEWIFSNGPEPGYDK--NGHDGGTRFRFSGDYALTQD 86
Cdd:COG3203     2 LLALAVAAALAGAAHA---------QSSV-------TLYGRVDAGVEYVDNGGGSLTRltSGGDSGSRLGFKGSEDLGGG 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012  87 TSIIGYYEWGVDLAHALSwdghynEDGKRDYQRQLYAGFKDDRYGTLTYGHQYGIYYSVVGiksdVWDNDGHAGGTGIGI 166
Cdd:COG3203    66 LKAIFQLESGFNADTGTS------GGGGRLFGRQAYVGLKGDDFGTLTLGRQYTPLYDVVG----AFDPFGDSGDAGNLA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 167 SGD-YDGGNKPKNSIKYTN-DFGPVTLYANYLLPEDDLHTADNliyrrkGGGGLGFDYKvTKDFTFSAAYSYTDakiKDN 244
Cdd:COG3203   136 GDDnLAGTGRADNAIKYRSpNFGGLTFGAQYSFGEDAGSSSNG------RGYGAGLTYA-NGPLSLGAAYQQSN---DAQ 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 245 LYSEKDYHQQLSGTALTWQPNNWYIVGTASYYKDYVPSTrqrtlshFFAGDGYGLEGFVGYTFNidkPFLKSIQPYVAAD 324
Cdd:COG3203   206 GATAGGDDADAWGLGASYDFGNLKLAAGYGQTKNDDAGG-------AGNAKADGYELGASYPFG---PALTLSASYGYTD 275
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2734168012 325 SLRLKGDeaYHANHVYLGAGTTIGYGLSVYVERTLANSSDN 365
Cdd:COG3203   276 AKDGADD--DDANQYALGADYALSKRTSLYAEYGYNDNDGN 314
gram_neg_porins cd00342
Porins form aqueous channels for the diffusion of small hydrophillic molecules across the ...
43-311 2.99e-19

Porins form aqueous channels for the diffusion of small hydrophillic molecules across the outer membrane. Individual 16-strand anti-parallel beta-barrels form a central pore, and trimerizes thru mainly hydrophobic interactions at the interface. Trimers are stabilized by hytrophillic clamping of Loop L2. Loop 3 bends into the pore, creating an elliptical constriction of about 7 x 11A, large enough to allow passage of a glucose molecule without steric hindrance. Removal of the C-terminal residue (usuallly F) destabilizes the trimer and removal of the 16th beta-sheet abolishes trimerization. Unlike typical membrane proteins, porins lack long hydrophobic stretches. Short turns are found at the smooth, periplasmic end, longer irregular loops are found at the rough, extracellular end. C-terminal residue forms salt bridge with N-terminus.


Pssm-ID: 238208 [Multi-domain]  Cd Length: 329  Bit Score: 87.43  E-value: 2.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012  43 SLKVGGSIRPEWIFSN---GPEPGYDKNGHDGGTRFRFSGDYALTQDTSIIGYYEWGVDLahalswDGHYNEDGKRDYQR 119
Cdd:cd00342     2 SVTLYGRIDAGVEYVNnagGGGAGQMTSGGNNGSRWGLRGSEDLGGGLKAIFQLESGFNL------NTGALGQGGRLFGR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 120 QLYAGFKDDRYGTLTYGHQYGIYYSVVGIKSdvwDNDGHAGGTGIGISGDYDGGNKPKNSIKYTN-DFGPVTLYANYLLP 198
Cdd:cd00342    76 QAYVGLSSDTYGTLTLGRQYTPLYDVLGTTD---PFGGSGGGSAPGDGDNLAGTGRANNSVKYTSpFFGGLTFGAMYAFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 199 EDDLHTADNLIYrrkgggGLGFDYKvTKDFTFSAAYSYTDAKIKDNLYSEKDYHQQLSGTALTWQPNNWYIVGTASYYK- 277
Cdd:cd00342   153 NQAGSTSNGRGY------GAGLSYE-NGPLSLGAAYDQQRNGGGAAGGAAGATSQRAYGAGASYDFGGLKLGAGYTNTRn 225
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2734168012 278 DYVPSTRQRTLSHFFAGDGY----GLEGFVGYTFNIDK 311
Cdd:cd00342   226 DNGGGGGSAKFNGYELGATYqltpALRLGAAYYYTKDR 263
Porin_4 pfam13609
Gram-negative porin;
39-243 4.01e-08

Gram-negative porin;


Pssm-ID: 433346 [Multi-domain]  Cd Length: 311  Bit Score: 54.37  E-value: 4.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012  39 LAPLSLKVGGSIRPEWIFSNGPEPG---YDKNGHDGGTRFRFSGdyalTQDTSIIGYYEWGVDLAHALSWDGHYNedgkr 115
Cdd:pfam13609  13 AAQSSVTLYGSADAGVGYVNGGAAGagaDGETGLDSNSRIGFGG----SEELDNGLGFGASFELEAGFNGAGGFN----- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 116 dyQRQLYAGFKDDrYGTLTYGHQYGIYYSVVGIKSDVWDNDGHAGGTGIGISGDYDGGNKPKNSI-KYTNDFGPVTLYAN 194
Cdd:pfam13609  84 --NRQAYVGLSGG-FGTVTLGRQDGAFDEAGVDYDFDGGSLGDSGYDGSGLSGSAGFDGRDSNSIiYYSPKFGGFTAGAS 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2734168012 195 YLLPEDD------LHTADNLIYRRKGGGGLGFDYKVTkDFTFSAAYSYTDAKIKD 243
Cdd:pfam13609 161 YAFGEDGntngnnGGVAGDSNDTDGYGLGAGYDFGGV-GFSVAAAYQQTDNEGGD 214
por_somb NF033921
iron uptake porin; Proteins of this family have typical porin structures. It has been reported ...
207-310 7.58e-04

iron uptake porin; Proteins of this family have typical porin structures. It has been reported that Synechococcus outer membrane (Som) porins (SomA and SomB) are involved in iron uptake in cyanobacterium Synechococcus.


Pssm-ID: 468246 [Multi-domain]  Cd Length: 481  Bit Score: 41.57  E-value: 7.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 207 NLIYRRKGGGGLGFDYKVTKDFTFSAAYSYTDAkikdNLYSEK------DYHqqlSGTALTWQPNNWYIVGtASYYKDYV 280
Cdd:NF033921  249 NPLYRRGPGGGAGVNWQISDNLSLTLGYLAGDP----NDPDEGnglfngSYN---ALAQLAFYPEQGIALG-LTYSHSYF 320
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2734168012 281 PSTRQ-------RTLSHF-F------AGDGYGLEGFVGYTFNID 310
Cdd:NF033921  321 PGGNVdltgstgSALANRpFgnniatSADIFGLQGYYRITPNFQ 364
Autotransporter smart00869
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ...
200-331 1.21e-03

Autotransporter beta-domain; Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type IV pathway was first described for the IgA1 protease. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C-terminus of the proteins it occurs in. The N-terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different peptidase is used and in some cases no cleavage occurs.


Pssm-ID: 214872 [Multi-domain]  Cd Length: 268  Bit Score: 40.25  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012  200 DDLHTADNLIYRRKGGGG-LGFDYKVTKDFT----FSAAYSYTDAKIKDNLYSEKDYHQ--QLSGTALTWQPNNWYIVGT 272
Cdd:smart00869  11 DSSGSGGSAGFDYDSYGLqLGADYRLSDNGNlslgFAAGYGNSKVDFSGNKGSGKGDVDsyGLGLYAGYSLGNGLYLDAQ 90
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2734168012  273 ASY------YKDYVPSTRQRTLSHFFAGDGYGLEGFVGYTFNIDKPFlkSIQPYVAADSLRLKGD 331
Cdd:smart00869  91 LGYgrsdndTKRKVTLGGAGRAKGSYDGTGYGASLEAGYRFYLGGGL--TLTPFAGLAYSRVRQD 153
 
Name Accession Description Interval E-value
OmpC COG3203
Outer membrane porin OmpC/OmpF/PhoE [Cell wall/membrane/envelope biogenesis];
9-365 3.71e-30

Outer membrane porin OmpC/OmpF/PhoE [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442436 [Multi-domain]  Cd Length: 336  Bit Score: 118.18  E-value: 3.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012   9 FIGGVLLSALSAGAQAeitildknpQSNVllaplslKVGGSIRPEWIFSNGPEPGYDK--NGHDGGTRFRFSGDYALTQD 86
Cdd:COG3203     2 LLALAVAAALAGAAHA---------QSSV-------TLYGRVDAGVEYVDNGGGSLTRltSGGDSGSRLGFKGSEDLGGG 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012  87 TSIIGYYEWGVDLAHALSwdghynEDGKRDYQRQLYAGFKDDRYGTLTYGHQYGIYYSVVGiksdVWDNDGHAGGTGIGI 166
Cdd:COG3203    66 LKAIFQLESGFNADTGTS------GGGGRLFGRQAYVGLKGDDFGTLTLGRQYTPLYDVVG----AFDPFGDSGDAGNLA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 167 SGD-YDGGNKPKNSIKYTN-DFGPVTLYANYLLPEDDLHTADNliyrrkGGGGLGFDYKvTKDFTFSAAYSYTDakiKDN 244
Cdd:COG3203   136 GDDnLAGTGRADNAIKYRSpNFGGLTFGAQYSFGEDAGSSSNG------RGYGAGLTYA-NGPLSLGAAYQQSN---DAQ 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 245 LYSEKDYHQQLSGTALTWQPNNWYIVGTASYYKDYVPSTrqrtlshFFAGDGYGLEGFVGYTFNidkPFLKSIQPYVAAD 324
Cdd:COG3203   206 GATAGGDDADAWGLGASYDFGNLKLAAGYGQTKNDDAGG-------AGNAKADGYELGASYPFG---PALTLSASYGYTD 275
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2734168012 325 SLRLKGDeaYHANHVYLGAGTTIGYGLSVYVERTLANSSDN 365
Cdd:COG3203   276 AKDGADD--DDANQYALGADYALSKRTSLYAEYGYNDNDGN 314
gram_neg_porins cd00342
Porins form aqueous channels for the diffusion of small hydrophillic molecules across the ...
43-311 2.99e-19

Porins form aqueous channels for the diffusion of small hydrophillic molecules across the outer membrane. Individual 16-strand anti-parallel beta-barrels form a central pore, and trimerizes thru mainly hydrophobic interactions at the interface. Trimers are stabilized by hytrophillic clamping of Loop L2. Loop 3 bends into the pore, creating an elliptical constriction of about 7 x 11A, large enough to allow passage of a glucose molecule without steric hindrance. Removal of the C-terminal residue (usuallly F) destabilizes the trimer and removal of the 16th beta-sheet abolishes trimerization. Unlike typical membrane proteins, porins lack long hydrophobic stretches. Short turns are found at the smooth, periplasmic end, longer irregular loops are found at the rough, extracellular end. C-terminal residue forms salt bridge with N-terminus.


Pssm-ID: 238208 [Multi-domain]  Cd Length: 329  Bit Score: 87.43  E-value: 2.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012  43 SLKVGGSIRPEWIFSN---GPEPGYDKNGHDGGTRFRFSGDYALTQDTSIIGYYEWGVDLahalswDGHYNEDGKRDYQR 119
Cdd:cd00342     2 SVTLYGRIDAGVEYVNnagGGGAGQMTSGGNNGSRWGLRGSEDLGGGLKAIFQLESGFNL------NTGALGQGGRLFGR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 120 QLYAGFKDDRYGTLTYGHQYGIYYSVVGIKSdvwDNDGHAGGTGIGISGDYDGGNKPKNSIKYTN-DFGPVTLYANYLLP 198
Cdd:cd00342    76 QAYVGLSSDTYGTLTLGRQYTPLYDVLGTTD---PFGGSGGGSAPGDGDNLAGTGRANNSVKYTSpFFGGLTFGAMYAFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 199 EDDLHTADNLIYrrkgggGLGFDYKvTKDFTFSAAYSYTDAKIKDNLYSEKDYHQQLSGTALTWQPNNWYIVGTASYYK- 277
Cdd:cd00342   153 NQAGSTSNGRGY------GAGLSYE-NGPLSLGAAYDQQRNGGGAAGGAAGATSQRAYGAGASYDFGGLKLGAGYTNTRn 225
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2734168012 278 DYVPSTRQRTLSHFFAGDGY----GLEGFVGYTFNIDK 311
Cdd:cd00342   226 DNGGGGGSAKFNGYELGATYqltpALRLGAAYYYTKDR 263
Porin_4 pfam13609
Gram-negative porin;
39-243 4.01e-08

Gram-negative porin;


Pssm-ID: 433346 [Multi-domain]  Cd Length: 311  Bit Score: 54.37  E-value: 4.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012  39 LAPLSLKVGGSIRPEWIFSNGPEPG---YDKNGHDGGTRFRFSGdyalTQDTSIIGYYEWGVDLAHALSWDGHYNedgkr 115
Cdd:pfam13609  13 AAQSSVTLYGSADAGVGYVNGGAAGagaDGETGLDSNSRIGFGG----SEELDNGLGFGASFELEAGFNGAGGFN----- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 116 dyQRQLYAGFKDDrYGTLTYGHQYGIYYSVVGIKSDVWDNDGHAGGTGIGISGDYDGGNKPKNSI-KYTNDFGPVTLYAN 194
Cdd:pfam13609  84 --NRQAYVGLSGG-FGTVTLGRQDGAFDEAGVDYDFDGGSLGDSGYDGSGLSGSAGFDGRDSNSIiYYSPKFGGFTAGAS 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2734168012 195 YLLPEDD------LHTADNLIYRRKGGGGLGFDYKVTkDFTFSAAYSYTDAKIKD 243
Cdd:pfam13609 161 YAFGEDGntngnnGGVAGDSNDTDGYGLGAGYDFGGV-GFSVAAAYQQTDNEGGD 214
Autotransporter pfam03797
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ...
210-331 2.71e-06

Autotransporter beta-domain; Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type V pathway was first described for the IgA1 protease. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C terminus of the proteins it occurs in. The N terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different protease is used and in some cases no cleavage occurs.


Pssm-ID: 461054 [Multi-domain]  Cd Length: 255  Bit Score: 48.15  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 210 YRRKGGGG-LGFDYKVTKDFTFSAA--YSYTDAKIKDNLYSEKDYHQQLSGTALTWQPNNWYIVGTASYYKDYVPSTRQR 286
Cdd:pfam03797  21 YDADTGGLqVGADYRLGDNLRLGVAfgYSRSDADVDGRGGSGDSDSYSLGLYGTYYGDGGWYLDGGLGYGWHDNDTRRSV 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2734168012 287 TLSHFFA-------GDGYGLEGFVGYTFNIDKPFlkSIQPYVAADSLRLKGD 331
Cdd:pfam03797 101 DLGGFSEtakgdydGNGFGASLEAGYRFALGGGW--TLEPFAGLAYVRLRLD 150
por_somb NF033921
iron uptake porin; Proteins of this family have typical porin structures. It has been reported ...
207-310 7.58e-04

iron uptake porin; Proteins of this family have typical porin structures. It has been reported that Synechococcus outer membrane (Som) porins (SomA and SomB) are involved in iron uptake in cyanobacterium Synechococcus.


Pssm-ID: 468246 [Multi-domain]  Cd Length: 481  Bit Score: 41.57  E-value: 7.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012 207 NLIYRRKGGGGLGFDYKVTKDFTFSAAYSYTDAkikdNLYSEK------DYHqqlSGTALTWQPNNWYIVGtASYYKDYV 280
Cdd:NF033921  249 NPLYRRGPGGGAGVNWQISDNLSLTLGYLAGDP----NDPDEGnglfngSYN---ALAQLAFYPEQGIALG-LTYSHSYF 320
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2734168012 281 PSTRQ-------RTLSHF-F------AGDGYGLEGFVGYTFNID 310
Cdd:NF033921  321 PGGNVdltgstgSALANRpFgnniatSADIFGLQGYYRITPNFQ 364
Autotransporter smart00869
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ...
200-331 1.21e-03

Autotransporter beta-domain; Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type IV pathway was first described for the IgA1 protease. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C-terminus of the proteins it occurs in. The N-terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different peptidase is used and in some cases no cleavage occurs.


Pssm-ID: 214872 [Multi-domain]  Cd Length: 268  Bit Score: 40.25  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734168012  200 DDLHTADNLIYRRKGGGG-LGFDYKVTKDFT----FSAAYSYTDAKIKDNLYSEKDYHQ--QLSGTALTWQPNNWYIVGT 272
Cdd:smart00869  11 DSSGSGGSAGFDYDSYGLqLGADYRLSDNGNlslgFAAGYGNSKVDFSGNKGSGKGDVDsyGLGLYAGYSLGNGLYLDAQ 90
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2734168012  273 ASY------YKDYVPSTRQRTLSHFFAGDGYGLEGFVGYTFNIDKPFlkSIQPYVAADSLRLKGD 331
Cdd:smart00869  91 LGYgrsdndTKRKVTLGGAGRAKGSYDGTGYGASLEAGYRFYLGGGL--TLTPFAGLAYSRVRQD 153
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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