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Database: UniProt
Entry: A0A0S1XVN7_9BORD
LinkDB: A0A0S1XVN7_9BORD
Original site: A0A0S1XVN7_9BORD 
ID   A0A0S1XVN7_9BORD        Unreviewed;       537 AA.
AC   A0A0S1XVN7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:ALM81810.1};
GN   ORFNames=ASB57_01485 {ECO:0000313|EMBL:ALM81810.1};
OS   Bordetella sp. N.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM81810.1, ECO:0000313|Proteomes:UP000064621};
RN   [1] {ECO:0000313|EMBL:ALM81810.1, ECO:0000313|Proteomes:UP000064621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N {ECO:0000313|EMBL:ALM81810.1,
RC   ECO:0000313|Proteomes:UP000064621};
RA   Hou L.;
RT   "Draft genome of Bordetella sp. N.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP013111; ALM81810.1; -; Genomic_DNA.
DR   RefSeq; WP_057649936.1; NZ_CP013111.1.
DR   AlphaFoldDB; A0A0S1XVN7; -.
DR   STRING; 1746199.ASB57_01485; -.
DR   OrthoDB; 9806477at2; -.
DR   Proteomes; UP000064621; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR024478; HlyB_4HB_MCP.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   PANTHER; PTHR32089:SF119; METHYL-ACCEPTING CHEMOTAXIS PROTEIN TLPQ; 1.
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; 2.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064621};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          208..260
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          265..501
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   537 AA;  58108 MW;  8C21CBA96104B611 CRC64;
     MKNMTLRQRL LASFAAILVI MLLMASVDYN RLLAIDTEAQ AINDDSLPGL QSSARLLAAW
     QKGYEVLRQG VARQTPAPAL RDALDQADAG MNEQLHKYSQ SVFILDDREV YETLLKTVNA
     YRQARAGVIT SLQDADIPRA RAQLAEGVTT IYNSGRTQLE QMVEENSTRA DRSVEHILKT
     LRHAQWILLA GLLLALLAAA TFAVVLTRAI NGPMLKIVDS LDRFGNGDLS ARLRLARKDE
     FGAIETGFNR MADELTELVG KAQRSAIQVA TSVTEIAATS RQQQATASEV ASTTTEIGAT
     SREIAATARD LVRTMSEVSA AADQTAALAD GGHHDLSRME HTMRSVVDAA GTVNGKLGVL
     NEKAGNINQV VTTINKVADQ TNLLSLNAAI EAEKAGEYGR GFVVVATEIR RLADQTAVAT
     YDIEQIVREI QSSVAAGVMG MDKFSEEVRR GMNDMQQVGE QLSQIIQHVQ TLAPRVQVVN
     EGMQAQATGA EQINQALTQL ADATQQTVES LRQSSLAIDD LNTVAGDLRG GVTRFKL
//
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