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: | O51918 |
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| Protein Name: | VceA |
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| Length: | 395 |
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| Molecular Weight: | 42449.00 |
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| Species: | Vibrio cholerae [666] |
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| Number of TMSs: | 3 |
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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: |
PF00529
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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: MNSNNSNTEF DGVRARQSRK KGFLGLAAAI VVAGGSYALY WHFIGSRYIS TDNAYAAAEI
61: AEVTPAVGRD YRASECRWIP STSTGDVLVQ LDDTDARLAL LQAEADLALA KRRVRSYLAN
121: DEGLSAMVEA QEANEQRVKA QLKAAQADFE RAKIDLSRRE DLVASGSVSG EELTNAKTGF
181: AQAQANLNAA KAAMAQAQAT KLSTIGSQKA NAALTDNTTV DSNPEVLLAK ARYEQAKIDL
241: ERTVIRAPIS GIVAKRQVQV GRRVQVGMPL MTVVPTDHIY VDANFKEVEL RDVKVGQPVT
301: LTADLYGDDV TYHGVVAGFS GGTGSAFSMI PAQNATGNWI KVVQRLPIRI ELDPKDLQAY
361: PLQVGLSMVA TIDTAGTTDP QTLVQYRAAK VSEQG