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Conserved domains on  [gi|4099398|gb|AAD00617|]
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outer membrane lipoprotein [Actinobacillus pleuropneumoniae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA03377 super family cl31823
EBNA-3C; Provisional
 38-111 3.32e-04

EBNA-3C; Provisional


The actual alignment was detected with superfamily member PHA03377:

Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 42.73  E-value: 3.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4099398     38 PKV---DMSAPKAEQPKKEevPQADNSKAEEPKEMAPQVDSPKAEEPKNMAPQMGNPKLNDPQVMAPKMDNPQKDAP 111
Cdd:PHA03377  553 PKVspsDRGPPKASPPVMA--PPSTGPRVMATPSTGPRDMAPPSTGPRQQAKCKDGPPASGPHEKQPPSSAPRDMAP 627
TbpB_B_D super family cl03152
C-lobe and N-lobe beta barrels of Tf-binding protein B; Bacterial lipoproteins represent a ...
 233-356 1.46e-03

C-lobe and N-lobe beta barrels of Tf-binding protein B; Bacterial lipoproteins represent a large group of specialized membrane proteins that perform a variety of functions including maintenance and stabilization of the cell envelope, protein targeting and transit to the outer membrane, membrane biogenesis, and cell adherence. Pathogenic Gram-negative bacteria within the Neisseriaceae and Pasteurellaceae families rely on a specialized uptake system, characterized by an essential surface receptor complex that acquires iron from host transferrin (Tf) and transports the iron across the outer membrane. They have an iron uptake system composed of surface exposed lipoprotein, Tf-binding protein B (TbpB), and an integral outer-membrane protein, Tf-binding protein A (TbpA), that together function to extract iron from the host iron binding glycoprotein (Tf). TbpB is a bilobed (N and C lobe) lipid-anchored protein with each lobe consisting of an eight-stranded beta barrel flanked by a "handle" domain made up of four (N lobe) or eight (C lobe) beta strands. TbpB extends from the outer membrane surface by virtue of an N-terminal peptide region that is anchored to the outer membrane by fatty acyl chains on the N-terminal cysteine and is involved in the initial capture of iron-loaded Tf. This domain family is found in C and N lobe eight stranded beta barrel region of TbpB proteins. The eight-stranded barrel domains in N and C lobe draw comparisons to eight-stranded beta barrel outer-membrane protein W (OmpW). However, the barrel domains of TbpB have the hydrophobic residues line the inner surface of the beta barrels to create a stable hydrophobic core.


The actual alignment was detected with superfamily member pfam01298:

Pssm-ID: 470752  Cd Length: 126  Bit Score: 38.09  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4099398    233 TKSISYKG---------DMFYSYKDVGNQKLKASVEASYDDVTKKVSMKVFGENNdywklgefgrtnllenQVTGAKVGE 303
Cdd:pfam01298   4 SGTATYKGhalfytinnSYHGGGGGDNNGEAGNTAEFDVDFGNKTLTGKLYNKDG----------------DEPDKPVNI 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 4099398    304 DGTIINGTLYSKIDNFPLKLTPDANFSGGIFGKNGEVLAGSAIS----EKWQGVIGA 356
Cdd:pfam01298  68 DANINGNRFSGTAKATDKGGDDDASVEGGFYGPNAEELGGSFNSlsedDKVGGVFGA 124
 
Name Accession Description Interval E-value
PHA03377 PHA03377
EBNA-3C; Provisional
 38-111 3.32e-04

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 42.73  E-value: 3.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4099398     38 PKV---DMSAPKAEQPKKEevPQADNSKAEEPKEMAPQVDSPKAEEPKNMAPQMGNPKLNDPQVMAPKMDNPQKDAP 111
Cdd:PHA03377  553 PKVspsDRGPPKASPPVMA--PPSTGPRVMATPSTGPRDMAPPSTGPRQQAKCKDGPPASGPHEKQPPSSAPRDMAP 627
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 31-114 1.14e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.91  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4099398    31 KPNSElTPKVDMSaPKAEQPKKEEVPQADNSKAE------EPK-EMAPQVDSPKAEEPknmaPQMGNPKLN-DPQVMAPK 102
Cdd:NF033839 322 KPQLE-KPKPEVK-PQPEKPKPEVKPQLETPKPEvkpqpeKPKpEVKPQPEKPKPEVK----PQPETPKPEvKPQPEKPK 395

                         90
                 ....*....|...
gi 4099398   103 MD-NPQKDAPKGE 114
Cdd:NF033839 396 PEvKPQPEKPKPE 408
TbpB_B_D pfam01298
C-lobe and N-lobe beta barrels of Tf-binding protein B; Bacterial lipoproteins represent a ...
 233-356 1.46e-03

C-lobe and N-lobe beta barrels of Tf-binding protein B; Bacterial lipoproteins represent a large group of specialized membrane proteins that perform a variety of functions including maintenance and stabilization of the cell envelope, protein targeting and transit to the outer membrane, membrane biogenesis, and cell adherence. Pathogenic Gram-negative bacteria within the Neisseriaceae and Pasteurellaceae families rely on a specialized uptake system, characterized by an essential surface receptor complex that acquires iron from host transferrin (Tf) and transports the iron across the outer membrane. They have an iron uptake system composed of surface exposed lipoprotein, Tf-binding protein B (TbpB), and an integral outer-membrane protein, Tf-binding protein A (TbpA), that together function to extract iron from the host iron binding glycoprotein (Tf). TbpB is a bilobed (N and C lobe) lipid-anchored protein with each lobe consisting of an eight-stranded beta barrel flanked by a "handle" domain made up of four (N lobe) or eight (C lobe) beta strands. TbpB extends from the outer membrane surface by virtue of an N-terminal peptide region that is anchored to the outer membrane by fatty acyl chains on the N-terminal cysteine and is involved in the initial capture of iron-loaded Tf. This domain family is found in C and N lobe eight stranded beta barrel region of TbpB proteins. The eight-stranded barrel domains in N and C lobe draw comparisons to eight-stranded beta barrel outer-membrane protein W (OmpW). However, the barrel domains of TbpB have the hydrophobic residues line the inner surface of the beta barrels to create a stable hydrophobic core.


Pssm-ID: 426188  Cd Length: 126  Bit Score: 38.09  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4099398    233 TKSISYKG---------DMFYSYKDVGNQKLKASVEASYDDVTKKVSMKVFGENNdywklgefgrtnllenQVTGAKVGE 303
Cdd:pfam01298   4 SGTATYKGhalfytinnSYHGGGGGDNNGEAGNTAEFDVDFGNKTLTGKLYNKDG----------------DEPDKPVNI 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 4099398    304 DGTIINGTLYSKIDNFPLKLTPDANFSGGIFGKNGEVLAGSAIS----EKWQGVIGA 356
Cdd:pfam01298  68 DANINGNRFSGTAKATDKGGDDDASVEGGFYGPNAEELGGSFNSlsedDKVGGVFGA 124
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 37-114 1.63e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.52  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4099398    37 TPKVDMSaPKAEQPKKEEVPQADNSK------AEEPK-EMAPQVDSPKAEEPknmaPQMGNPKLN-DPQVMAPKMD-NPQ 107
Cdd:NF033839 294 APKPGMQ-PSPQPEKKEVKPEPETPKpevkpqLEKPKpEVKPQPEKPKPEVK----PQLETPKPEvKPQPEKPKPEvKPQ 368


                 ....*..
gi 4099398   108 KDAPKGE 114
Cdd:NF033839 369 PEKPKPE 375
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 31-123 2.44e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 39.75  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4099398    31 KPNSElTPKVDMSaPKAEQPKKEEVPQADNSK------AEEPK-EMAPQVDSPKAEEP-------KNMAPQMGNPKLN-D 95
Cdd:NF033839 399 KPQPE-KPKPEVK-PQPEKPKPEVKPQPEKPKpevkpqPEKPKpEVKPQPEKPKPEVKpqpetpkPEVKPQPEKPKPEvK 476

                         90       100       110
                 ....*....|....*....|....*....|...
gi 4099398    96 PQVMAPKMDN--PQKDAPK---GEELSKDKSNA 123
Cdd:NF033839 477 PQPEKPKPDNskPQADDKKpstPNNLSKDKQPS 509
 
Name Accession Description Interval E-value
PHA03377 PHA03377
EBNA-3C; Provisional
 38-111 3.32e-04

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 42.73  E-value: 3.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4099398     38 PKV---DMSAPKAEQPKKEevPQADNSKAEEPKEMAPQVDSPKAEEPKNMAPQMGNPKLNDPQVMAPKMDNPQKDAP 111
Cdd:PHA03377  553 PKVspsDRGPPKASPPVMA--PPSTGPRVMATPSTGPRDMAPPSTGPRQQAKCKDGPPASGPHEKQPPSSAPRDMAP 627
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 31-114 1.14e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.91  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4099398    31 KPNSElTPKVDMSaPKAEQPKKEEVPQADNSKAE------EPK-EMAPQVDSPKAEEPknmaPQMGNPKLN-DPQVMAPK 102
Cdd:NF033839 322 KPQLE-KPKPEVK-PQPEKPKPEVKPQLETPKPEvkpqpeKPKpEVKPQPEKPKPEVK----PQPETPKPEvKPQPEKPK 395

                         90
                 ....*....|...
gi 4099398   103 MD-NPQKDAPKGE 114
Cdd:NF033839 396 PEvKPQPEKPKPE 408
TbpB_B_D pfam01298
C-lobe and N-lobe beta barrels of Tf-binding protein B; Bacterial lipoproteins represent a ...
 233-356 1.46e-03

C-lobe and N-lobe beta barrels of Tf-binding protein B; Bacterial lipoproteins represent a large group of specialized membrane proteins that perform a variety of functions including maintenance and stabilization of the cell envelope, protein targeting and transit to the outer membrane, membrane biogenesis, and cell adherence. Pathogenic Gram-negative bacteria within the Neisseriaceae and Pasteurellaceae families rely on a specialized uptake system, characterized by an essential surface receptor complex that acquires iron from host transferrin (Tf) and transports the iron across the outer membrane. They have an iron uptake system composed of surface exposed lipoprotein, Tf-binding protein B (TbpB), and an integral outer-membrane protein, Tf-binding protein A (TbpA), that together function to extract iron from the host iron binding glycoprotein (Tf). TbpB is a bilobed (N and C lobe) lipid-anchored protein with each lobe consisting of an eight-stranded beta barrel flanked by a "handle" domain made up of four (N lobe) or eight (C lobe) beta strands. TbpB extends from the outer membrane surface by virtue of an N-terminal peptide region that is anchored to the outer membrane by fatty acyl chains on the N-terminal cysteine and is involved in the initial capture of iron-loaded Tf. This domain family is found in C and N lobe eight stranded beta barrel region of TbpB proteins. The eight-stranded barrel domains in N and C lobe draw comparisons to eight-stranded beta barrel outer-membrane protein W (OmpW). However, the barrel domains of TbpB have the hydrophobic residues line the inner surface of the beta barrels to create a stable hydrophobic core.


Pssm-ID: 426188  Cd Length: 126  Bit Score: 38.09  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4099398    233 TKSISYKG---------DMFYSYKDVGNQKLKASVEASYDDVTKKVSMKVFGENNdywklgefgrtnllenQVTGAKVGE 303
Cdd:pfam01298   4 SGTATYKGhalfytinnSYHGGGGGDNNGEAGNTAEFDVDFGNKTLTGKLYNKDG----------------DEPDKPVNI 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 4099398    304 DGTIINGTLYSKIDNFPLKLTPDANFSGGIFGKNGEVLAGSAIS----EKWQGVIGA 356
Cdd:pfam01298  68 DANINGNRFSGTAKATDKGGDDDASVEGGFYGPNAEELGGSFNSlsedDKVGGVFGA 124
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 37-114 1.63e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.52  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4099398    37 TPKVDMSaPKAEQPKKEEVPQADNSK------AEEPK-EMAPQVDSPKAEEPknmaPQMGNPKLN-DPQVMAPKMD-NPQ 107
Cdd:NF033839 294 APKPGMQ-PSPQPEKKEVKPEPETPKpevkpqLEKPKpEVKPQPEKPKPEVK----PQLETPKPEvKPQPEKPKPEvKPQ 368


                 ....*..
gi 4099398   108 KDAPKGE 114
Cdd:NF033839 369 PEKPKPE 375
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 31-123 2.44e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 39.75  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4099398    31 KPNSElTPKVDMSaPKAEQPKKEEVPQADNSK------AEEPK-EMAPQVDSPKAEEP-------KNMAPQMGNPKLN-D 95
Cdd:NF033839 399 KPQPE-KPKPEVK-PQPEKPKPEVKPQPEKPKpevkpqPEKPKpEVKPQPEKPKPEVKpqpetpkPEVKPQPEKPKPEvK 476

                         90       100       110
                 ....*....|....*....|....*....|...
gi 4099398    96 PQVMAPKMDN--PQKDAPK---GEELSKDKSNA 123
Cdd:NF033839 477 PQPEKPKPDNskPQADDKKpstPNNLSKDKQPS 509
 
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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