| General information | | DisProt: | DP00400 | | Name: | Lipid A export ATP-binding/permease protein msbA | | Synonym(s): | MSBA_ECOLI
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P60752 | | UniGene: | | | SwissProt: | MSBA_ECOLI | | TrEMBL: | | | NCBI (GI): | 46397619 | | Source organism: | Escherichia coli | | Sequence length: | 582 | | Percent disordered: | 19% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MHNDKDLSTW QTFRRLWPTI APFKAGLIVA GVALILNAAS DTFMLSLLKP LLDDGFGKTD - 60
RSVLVWMPLV VIGLMILRGI TSYVSSYCIS WVSGKVVMTM RRRLFGHMMG MPVSFFDKQS - 120
TGTLLSRITY DSEQVASSSS GALITVVREG ASIIGLFIMM FYYSWQLSII LIVLAPIVSI - 180
AIRVVSKRFR NISKNMQNTM GQVTTSAEQM LKGHKEVLIF GGQEVETKRF DKVSNRMRLQ - 240
GMKMVSASSI SDPIIQLIAS LALAFVLYAA SFPSVMDSLT AGTITVVFSS MIALMRPLKS - 300
LTNVNAQFQR GMAACQTLFT ILDSEQEKDE GKRVIERATG DVEFRNVTFT YPGRDVPALR - 360
NINLKIPAGK TVALVGRSGS GKSTIASLIT RFYDIDEGEI LMDGHDLREY TLASLRNQVA - 420
LVSQNVHLFN DTVANNIAYA RTEQYSREQI EEAARMAYAM DFINKMDNGL DTVIGENGVL - 480
LSGGQRQRIA IARALLRDSP ILILDEATSA LDTESERAIQ AALDELQKNR TSLVIAHRLS - 540
TIEKADEIVV VEDGVIVERG THNDLLEHRG VYAQLHKMQF GQ
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| Functional narrative |
Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 58 - 63 | | Length: | 6 | | Region sequence: |
KTDRSV | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Entropic chain
| | Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- X-ray crystallography
| References:
- Chang G, Roth CB. "Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters." Science. 2001; 293(5536): 1793-800. PubMed: 11546864
| Comments:The electron densities are "diffuse" for amino acids 58 through 63.
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 208 - 236 | | Length: | 29 | | Region sequence: |
EQMLKGHKEVLIFGGQEVETKRFDKVSNR | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Substrate/ligand binding
| Detection methods:
- X-ray crystallography
| References:
- Chang G, Roth CB. "Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters." Science. 2001; 293(5536): 1793-800. PubMed: 11546864
| Comments:
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| Region 3 | | Type: | Disordered | | Name: | | | Location: | 341 - 418 | | Length: | 78 | | Region sequence: |
DVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEI
LMDGHDLREYTLASLRNQ | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography
| References:
- Chang G, Roth CB. "Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters." Science. 2001; 293(5536): 1793-800. PubMed: 11546864
| Comments:
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