2.A.1.3.24
The VceAB multidrug (hydrophobic compounds including deoxycholate (DOC), antibiotics, such as chloramphenicol and nalidixic acid, and the proton motive force uncoupler, cyanide carbonyl m-chlorophenylhydrazone (CCCP)) resistance pump (functions with outer membrane VceC (TC#1.B.17.3.6) or OprM (2.A.6.2.21), an OMF family member; The C-terminal domain of the Pseudomonas aeruginosa OprM and the
alpha-helical hairpin domain of Vibrio cholerae VceA play important
roles in recognition/specificity/recruitment in the assembly of a
functional, VceAB-OprM chimeric efflux pump (Bai et al., 2010).
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| Accession Number: | O51919 |
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| Protein Name: | VceB |
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| Length: | 511 |
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| Molecular Weight: | 55808.00 |
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| Species: | Vibrio cholerae [666] |
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| Number of TMSs: | 14 |
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| Location1 / Topology2 / Orientation3: |
Cell inner membrane1 / Multi-pass membrane protein2 |
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| Substrate |
chloramphenicol, nalidixic acid, deoxycholate, CCCP |
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| Pfam: |
PF07690
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[1] “Isolation and characterization of a putative multidrug resistance pump from Vibrio cholerae.” Colmer J.A. et.al. 9466256
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1: MSHNADNEMQ PLSGWALFFG ALCLAMANFL AILDTTIANV SVSNIAGSLG TSTSQGTYVI
61: TSYAVAEAIS VPLTGWLASR FGSIRVFVTC FLLFGVFSLL CGLANSMSTL VMFRVLLGFV
121: GGPLMPLSQT LMMRIFPKNK SHAAIGIWSM TTLVAPIMGP ILGGVLCDQL SWPYIFFIKM
181: PFAIAAALLC WKCVKKFETK TTHSKIDKVG LALLVVWVAA LQLMLDEGKD HDWFESSRIV
241: FLAVIAVIGF IAFLIWELTE RNPVVDLKVF RHRGYSISLV TLSLAFGAFF SISVVTPLWL
301: QIYMGYTATI SGHATASMGI LAVFLAPIVA NLSSKFDPRP FVFAGVMWLG LWTFMRGFNT
361: VDMTFSQISW PLFFQGIGMP LFFVPLTAIA LGSVKPHEME SAAGLMNFIR TLSGAFATSM
421: INTSWEHETR YVHAELAGLT DKAGVAAQAM QSSGMSAEQT RSAMDWILQN QSVMVATNQL
481: FIVIALIFVF AACMIWFAPK PKQAVDTSAV H