| General information | | DisProt: | DP00725 | | Name: | Type II secretion system protein M | | Synonym(s): | GSPM_VIBCH
Cholera toxin secretion protein EpsM
General secretion pathway protein M
T2SS protein M
| | First appeared in release: | Release 6.00 (07/01/2012) | | UniProt: | P41851 | | UniGene: | | | SwissProt: | GSPM_VIBCH | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) | | Sequence length: | 165 | | Percent disordered: | 28% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MKELLAPVQA WWRSVTPREQ KMVMGMGALT VLAIAYWGIW QPLSERTAQA QARLQTEKQL - 60
LSWVSENAND IVTLRAQGGS DAPSDQPLNQ VITNSTRQFN IELIRVQPRG EMMQVWIQPL - 120
PFSQLVSWIA YLQERQGVSV DAIDIDRGKV NGVVEVKRLQ LKRGG
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| Functional narrative |
Function: Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins (By similarity). Required for secretion of cholera toxin through the outer membrane.
Subcellular Location: Cell inner membrane (Probable).
SIMILARITY: Belongs to the GSP M family. Sequence=AAF95864.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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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: | N-terminal of periplasmic domain | | Location: | 44 - 85 | | Length: | 42 | | Region sequence: |
SERTAQAQARLQTEKQLLSWVSENANDIVTLRAQGGSDAPSD | | Modification type: | Fragment
| | PDB: | 1UV7:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | | | Functional subclasses: | | Detection methods:
- X-ray crystallography (277 K; pH: 8; EpsM fragment (aa 65-165) 1.5 uL; Sodium malonate (2.4-3.0M) 2.4 M; Tris 100 mM)
| References:
- Abendroth J, Rice AE, McLuskey K, Bagdasarian M, Hol WG. "The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: the simplest version of the ferredoxin fold." J. Mol. Biol.. 2004; 338(3): 585-96. PubMed: 15081815
| Comments:Abendroth et al (2004) used fragment aaS65-G165 of EpsM for crystallization experiments, but discussion of disorder includes S44-S85.
The authors discuss the possibility that in full-length EpsM, S44-R75 may belongs to a transmembrane helix, followed by a flexible linker at A76-Q86.
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| Region 2 | | Type: | Disordered | | Name: | loop | | Location: | 148 - 152 | | Length: | 5 | | Region sequence: |
GKVNG | | Modification type: | Fragment
| | PDB: | 1UV7:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | | | Functional subclasses: | | Detection methods:
- X-ray crystallography (277 K; pH: 8; EpsM fragment (aa 65-165) 1.5 uL; Sodium malonate (2.4-3.0M) 2.4 M; Tris 100 mM)
| References:
- Abendroth J, Rice AE, McLuskey K, Bagdasarian M, Hol WG. "The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: the simplest version of the ferredoxin fold." J. Mol. Biol.. 2004; 338(3): 585-96. PubMed: 15081815
| Comments:Abendroth et al (2004) used fragment aaS65-G165 of EpsM for crystallization experiments. They describe weak density at aa G148-G152.
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| Comments |
AV sent 6-21-2012 (PMID: 15081815)
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