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Protein

Methyl-accepting chemotaxis protein HlyB

Gene

hlyB

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation.By similarity

GO - Molecular functioni

  • signal transducer activity Source: UniProtKB-KW
  • transporter activity Source: TIGR

GO - Biological processi

  • chemotaxis Source: UniProtKB-KW
  • pathogenesis Source: TIGR
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Chemotaxis

Enzyme and pathway databases

BioCyciVCHO:VCA0220-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-accepting chemotaxis protein HlyB
Gene namesi
Name:hlyB
Ordered Locus Names:VC_A0220
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000584 Componenti: Chromosome 2

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010CytoplasmicSequence analysis
Transmembranei11 – 3121HelicalSequence analysisAdd
BLAST
Topological domaini32 – 199168PeriplasmicSequence analysisAdd
BLAST
Transmembranei200 – 22021HelicalSequence analysisAdd
BLAST
Topological domaini221 – 548328CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 548548Methyl-accepting chemotaxis protein HlyBPRO_0000013359Add
BLAST

Keywords - PTMi

Methylation

Interactioni

Protein-protein interaction databases

STRINGi243277.VCA0220.

Structurei

3D structure databases

ProteinModelPortaliP15492.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini218 – 27154HAMPPROSITE-ProRule annotationAdd
BLAST
Domaini276 – 512237Methyl-accepting transducerPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HAMP domain.PROSITE-ProRule annotation
Contains 1 methyl-accepting transducer domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4108N3W. Bacteria.
ENOG410ZWZ7. LUCA.
OMAiASRIPRM.
OrthoDBiEOG657J89.

Family and domain databases

InterProiIPR024478. 4HB_MCP.
IPR004090. Chemotax_Me-accpt_rcpt.
IPR003660. HAMP_dom.
IPR004089. MCPsignal_dom.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF12729. 4HB_MCP_1. 1 hit.
PF00672. HAMP. 1 hit.
PF00015. MCPsignal. 1 hit.
[Graphical view]
PRINTSiPR00260. CHEMTRNSDUCR.
SMARTiSM00304. HAMP. 1 hit.
SM00283. MA. 1 hit.
[Graphical view]
PROSITEiPS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
PS50885. HAMP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15492-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIINKFSLKW MLAIAVAIPA IALLFVAFTS LNTMSVMQAQ SNSLYANTAA
60 70 80 90 100
PMRAMAEATS RIPRMRVGID MMLLQETALK DAKGVLKRVE EARTEDIPEM
110 120 130 140 150
RQAMQVAVDS QVNPELKEQA RKLQARFEQM VREELEPMLQ AFANNDMTTA
160 170 180 190 200
QNIYRDKYAP TYGEMRKQAN QILDTLLQQA EQQNHASVES FEAGRTKQMV
210 220 230 240 250
IIAAGLIISF ITSLVIITNL RSRVAYLKDR MSSAAANLSL RTRLELDGND
260 270 280 290 300
ELCDIGKSFN AFIDKVHHSI EEVAENSKEL ATMASSVSQR AHMTQSNCAS
310 320 330 340 350
QRDRTVQVAT AIHELGATVS EIASNAAMAA DVAKQATLHS GEGKKVVGEV
360 370 380 390 400
QNRIQTLVNE LDNATQVVSS LATQINGISS TLDTIRSISE QTNLLALNAA
410 420 430 440 450
IEAARAGEQG RGFAVVADEV RTLASRSAAS TEEIQQVINR LQTESTRAVE
460 470 480 490 500
AMEKGRSQSD VVVEFSAKAN QSLTEINSQI DQINDQNIQV ATATEEQSTV
510 520 530 540
VEDINRNVED INQLTTETSH VADELSRASA SLQRLSSQLD KLVGSFEL
Length:548
Mass (Da):60,035
Last modified:December 1, 2000 - v2
Checksum:iE89211DD8038A2F4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221A → R in CAA68638 (PubMed:2162464).Curated
Sequence conflicti103 – 1031A → R in CAA68638 (PubMed:2162464).Curated
Sequence conflicti181 – 1822EQ → DR in CAA68638 (PubMed:2162464).Curated
Sequence conflicti330 – 3301A → R in CAA68638 (PubMed:2162464).Curated
Sequence conflicti334 – 3352KQ → NE in CAA68638 (PubMed:2162464).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00557 Genomic DNA. Translation: CAA68638.1.
AE003853 Genomic DNA. Translation: AAF96132.1.
PIRiB82486.
S15910.
RefSeqiNP_232619.1. NC_002506.1.
WP_000586206.1. NC_002506.1.

Genome annotation databases

EnsemblBacteriaiAAF96132; AAF96132; VC_A0220.
GeneIDi2612596.
KEGGivch:VCA0220.
PATRICi20085003. VBIVibCho83274_2853.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00557 Genomic DNA. Translation: CAA68638.1.
AE003853 Genomic DNA. Translation: AAF96132.1.
PIRiB82486.
S15910.
RefSeqiNP_232619.1. NC_002506.1.
WP_000586206.1. NC_002506.1.

3D structure databases

ProteinModelPortaliP15492.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VCA0220.

Protocols and materials databases

DNASUi2612596.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF96132; AAF96132; VC_A0220.
GeneIDi2612596.
KEGGivch:VCA0220.
PATRICi20085003. VBIVibCho83274_2853.

Phylogenomic databases

eggNOGiENOG4108N3W. Bacteria.
ENOG410ZWZ7. LUCA.
OMAiASRIPRM.
OrthoDBiEOG657J89.

Enzyme and pathway databases

BioCyciVCHO:VCA0220-MONOMER.

Family and domain databases

InterProiIPR024478. 4HB_MCP.
IPR004090. Chemotax_Me-accpt_rcpt.
IPR003660. HAMP_dom.
IPR004089. MCPsignal_dom.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF12729. 4HB_MCP_1. 1 hit.
PF00672. HAMP. 1 hit.
PF00015. MCPsignal. 1 hit.
[Graphical view]
PRINTSiPR00260. CHEMTRNSDUCR.
SMARTiSM00304. HAMP. 1 hit.
SM00283. MA. 1 hit.
[Graphical view]
PROSITEiPS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
PS50885. HAMP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the hlyB gene and its role in the production of the El Tor haemolysin of Vibrio cholerae O1."
    Alm R.A., Manning P.A.
    Mol. Microbiol. 4:413-425(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: El Tor O17 / Serotype O1.
  2. Manning P.A.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39315 / El Tor Inaba N16961.
  4. "Vibrio cholerae hlyB is a member of the chemotaxis receptor gene family."
    Jeffery C.J., Koshland D.E. Jr.
    Protein Sci. 2:1532-1535(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A MEMBER OF THE CHEMOTAXIS RECEPTOR FAMILY.

Entry informationi

Entry nameiHLYB_VIBCH
AccessioniPrimary (citable) accession number: P15492
Secondary accession number(s): Q9KMU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 1, 2000
Last modified: July 6, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be a pore or transmembrane transporter for hemolysin.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.