1MT0,1XEF


Conserved Protein Domain Family
ABCC_Hemolysin

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cd03252: ABCC_Hemolysin 
Click on image for an interactive view with Cn3D
ATP-binding cassette domain of hemolysin B, subfamily C
The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Statistics
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PSSM-Id: 213219
Aligned: 6 rows
Threshold Bit Score: 428.829
Created: 4-Aug-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:ATP binding site [chemical binding site]
Evidence:
  • Comment:Walker A, Walker B, Q-loop, D-loop, and H-loop form the nucleotide binding site
  • Structure:1XEF; Mg-ATP bound, 3.5A contacts
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                            ## ###                                    
1MT0_A       2 ITFRNIRFRYkpds-pviLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80   Escherichia coli
1XEF_D       2 ITFRNIRFRYkpds-pviLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80   Escherichia coli
AAF41764   503 ITFEHVDFRYkadg-rliLQDLNLRIRAGEVLGIVGRSGSGKSTLTKLVQRLYVPEQGRVLVDGNDLALAAPAWLRRQVG 581  Neisseria mening...
NP_772933  592 VVFEHATFRYradg-pevLHDVSFGVEPGQVVGIVGSSGSGKSTIGKLIQRLYVPESGRVLVDGVDLATVDLTWLRRQIG 670  Bradyrhizobium j...
P18770     471 IELDRVSFRYrpda-adaLRNVSLRIAPGEVVGVVGRSGSGKSTLTRLIQRMFVADRGRVLIDGHDIGIVDSASLRRQLG 549  Bordetella pertu...
CAI07029   780 IAFEGVYFRYggdetpyvLENISFEIKPGELVAIVGRSGSGKTTLAKLLVGFYPPTDGRIVVDGYDMATIDKEYYRAQVG 859  Azoarcus sp. EbN1
Feature 1         #                                                                            
1MT0_A      81 VVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160  Escherichia coli
1XEF_D      81 VVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160  Escherichia coli
AAF41764   582 VVLQENVLLNRSIRDNIALTDTGMPLERIIEAAKLAGAHEFIMELPEGYGTVVGEQGAGLSGGQRQRIAIARALITNPRI 661  Neisseria mening...
NP_772933  671 VVLQENVLFNRSIRENIALADPAMPMERVIEAASLAGAHDFILELPEGYDTIVGERGSSLSGGQRQRVAIARALITNPRI 750  Bradyrhizobium j...
P18770     550 VVLQESTLFNRSVRDNIALTRPGASMHEVVAAARLAGAHEFICQLPEGYDTMLGENGVGLSGGQRQRIGIARALIHRPRV 629  Bordetella pertu...
CAI07029   860 YVMQSNLLFSGTIAENIASGDEAPDRRRIEEVARMADAHAFIRKMPLGYEQIVGERGVGLSGGQIQRLCIARALYHDPRL 939  Azoarcus sp. EbN1
Feature 1         ##                              #                                           
1MT0_A     161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELlsepeslYSYLYQLQ 239  Escherichia coli
1XEF_D     161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAARLSTVKNADRIIVMEKGKIVEQGKHKELlsepeslYSYLYQLQ 239  Escherichia coli
AAF41764   662 LIFDEATSALDYESERAIMQNMQAICANRTVLIIAHRLSTVKTAHRIIAMDKGRIVEAGTQQELlakpngyYRYLYDLQ 740  Neisseria meningi...
NP_772933  751 LILDEATSALDYESERAIQQNMKRISAGRTVIVIAHRLSTVRNANRIITLEHGRIVEDGSHDELirs-ngrYANLHYLQ 828  Bradyrhizobium ja...
P18770     630 LILDEATSALDYESEHIIQRNMRDICDGRTVIIIAHRLSAVRCADRIVVMEGGEVAECGSHETLlaa-gglYARLQALQ 707  Bordetella pertussis
CAI07029   940 LVFDEATSALDTQSESNIISNMHDILAGRTAVVIAHRLSTIMRADKILVLYEGAIVEQGRHDELvdr-rgmYYQLVQKQ 1017 Azoarcus sp. EbN1

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