HLYB_VIBCH
ID HLYB_VIBCH Reviewed; 548 AA.
AC P15492; Q9KMU8;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Methyl-accepting chemotaxis protein HlyB;
GN Name=hlyB; OrderedLocusNames=VC_A0220;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=El Tor O17 / Serotype O1;
RX PubMed=2162464; DOI=10.1111/j.1365-2958.1990.tb00608.x;
RA Alm R.A., Manning P.A.;
RT "Characterization of the hlyB gene and its role in the production of the El
RT Tor haemolysin of Vibrio cholerae O1.";
RL Mol. Microbiol. 4:413-425(1990).
RN [2]
RP SEQUENCE REVISION.
RA Manning P.A.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [4]
RP IDENTIFICATION AS A MEMBER OF THE CHEMOTAXIS RECEPTOR FAMILY.
RX PubMed=8401237; DOI=10.1002/pro.5560020918;
RA Jeffery C.J., Koshland D.E. Jr.;
RT "Vibrio cholerae hlyB is a member of the chemotaxis receptor gene family.";
RL Protein Sci. 2:1532-1535(1993).
CC -!- FUNCTION: Chemotactic-signal transducers respond to changes in the
CC concentration of attractants and repellents in the environment,
CC transduce a signal from the outside to the inside of the cell, and
CC facilitate sensory adaptation through the variation of the level of
CC methylation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a pore or transmembrane
CC transporter for hemolysin. {ECO:0000305|PubMed:2162464}.
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DR EMBL; Y00557; CAA68638.1; -; Genomic_DNA.
DR EMBL; AE003853; AAF96132.1; -; Genomic_DNA.
DR PIR; B82486; B82486.
DR PIR; S15910; S15910.
DR RefSeq; NP_232619.1; NC_002506.1.
DR RefSeq; WP_000586206.1; NZ_LT906615.1.
DR AlphaFoldDB; P15492; -.
DR SMR; P15492; -.
DR STRING; 243277.VC_A0220; -.
DR DNASU; 2612596; -.
DR EnsemblBacteria; AAF96132; AAF96132; VC_A0220.
DR GeneID; 57741667; -.
DR KEGG; vch:VC_A0220; -.
DR PATRIC; fig|243277.26.peg.2853; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_27_6; -.
DR OMA; VEAQACA; -.
DR BioCyc; VCHO:VCA0220-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR000727; T_SNARE_dom.
DR Pfam; PF12729; 4HB_MCP_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Chemotaxis; Membrane; Methylation;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..548
FT /note="Methyl-accepting chemotaxis protein HlyB"
FT /id="PRO_0000013359"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..199
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..548
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 218..271
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 276..512
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT CONFLICT 22
FT /note="A -> R (in Ref. 1; CAA68638)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="A -> R (in Ref. 1; CAA68638)"
FT /evidence="ECO:0000305"
FT CONFLICT 181..182
FT /note="EQ -> DR (in Ref. 1; CAA68638)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="A -> R (in Ref. 1; CAA68638)"
FT /evidence="ECO:0000305"
FT CONFLICT 334..335
FT /note="KQ -> NE (in Ref. 1; CAA68638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 60035 MW; E89211DD8038A2F4 CRC64;
MIINKFSLKW MLAIAVAIPA IALLFVAFTS LNTMSVMQAQ SNSLYANTAA PMRAMAEATS
RIPRMRVGID MMLLQETALK DAKGVLKRVE EARTEDIPEM RQAMQVAVDS QVNPELKEQA
RKLQARFEQM VREELEPMLQ AFANNDMTTA QNIYRDKYAP TYGEMRKQAN QILDTLLQQA
EQQNHASVES FEAGRTKQMV IIAAGLIISF ITSLVIITNL RSRVAYLKDR MSSAAANLSL
RTRLELDGND ELCDIGKSFN AFIDKVHHSI EEVAENSKEL ATMASSVSQR AHMTQSNCAS
QRDRTVQVAT AIHELGATVS EIASNAAMAA DVAKQATLHS GEGKKVVGEV QNRIQTLVNE
LDNATQVVSS LATQINGISS TLDTIRSISE QTNLLALNAA IEAARAGEQG RGFAVVADEV
RTLASRSAAS TEEIQQVINR LQTESTRAVE AMEKGRSQSD VVVEFSAKAN QSLTEINSQI
DQINDQNIQV ATATEEQSTV VEDINRNVED INQLTTETSH VADELSRASA SLQRLSSQLD
KLVGSFEL
