ID Q7VXY0_BORPE Unreviewed; 563 AA. AC Q7VXY0; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 98. DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:CAE41880.1}; GN OrderedLocusNames=BP1591 {ECO:0000313|EMBL:CAE41880.1}; OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE41880.1, ECO:0000313|Proteomes:UP000002676}; RN [1] {ECO:0000313|Proteomes:UP000002676} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251 RC {ECO:0000313|Proteomes:UP000002676}; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., RA Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004429}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein CC family. {ECO:0000256|ARBA:ARBA00029447}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX640415; CAE41880.1; -; Genomic_DNA. DR RefSeq; NP_880324.1; NC_002929.2. DR AlphaFoldDB; Q7VXY0; -. DR STRING; 257313.BP1591; -. DR PaxDb; 257313-BP1591; -. DR KEGG; bpe:BP1591; -. DR PATRIC; fig|257313.5.peg.1708; -. DR eggNOG; COG0840; Bacteria. DR HOGENOM; CLU_000445_107_16_4; -. DR Proteomes; UP000002676; Chromosome. 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 CDD; cd06225; HAMP; 1. DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1. DR InterPro; IPR035440; 4HB_MCP_dom_sf. DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR004089; MCPsignal_dom. DR InterPro; IPR003122; Tar_rcpt_lig-bd. DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1. DR PANTHER; PTHR43531; PROTEIN ICFG; 1. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF00015; MCPsignal; 1. DR Pfam; PF02203; TarH; 1. DR PRINTS; PR00260; CHEMTRNSDUCR. DR SMART; SM00304; HAMP; 1. DR SMART; SM00283; MA; 1. DR SUPFAM; SSF47170; Aspartate receptor, ligand-binding domain; 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 Chemotaxis {ECO:0000256|ARBA:ARBA00022500}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Methylation {ECO:0000256|ARBA:ARBA00022481}; KW Reference proteome {ECO:0000313|Proteomes:UP000002676}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1..28 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 29..563 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004292720" FT TRANSMEM 192..214 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 216..268 FT /note="HAMP" FT /evidence="ECO:0000259|PROSITE:PS50885" FT DOMAIN 273..502 FT /note="Methyl-accepting transducer" FT /evidence="ECO:0000259|PROSITE:PS50111" SQ SEQUENCE 563 AA; 57761 MW; 212F019E2939CF17 CRC64; MRKKLKLAAA LSATLAFFVL LFAAAAGAGV AVLRDNQAAI EALGRGNIER ASDLGDTTSW LFQARAVLAD AKTYMEGGLE EQRDAALAQA ATLLEQVRAS QERLRANPEM AAQGASLYDE VLAGYDALAV QALAPLHAAL KGWNGIEANR LAERALPQAA ERYIEAVDAF QGYAREQGRA AVADAARVLE RMVLGAAALL ALVAVLAVVI RLGFRRAMLR PLTEAGRHFD RIADGDLTAA IAARGDNEIG ALYSAMRRMQ GGLTRAVESV RHGVEEIHTG SGEIAAGGVE MSGRTARQAG ALQEAAASMA ELAGTVRATA EHADQASRQA AGATELARQG GTAVAQVVAS MRDIASGAQR IAEIVGLVDS LAFQTNVLAL NAAVEAARAG PQGRGFAVVA GEVRSLAQRS AQAAREIKGL IDDSSARVAS GVQQVNLAGA TMGEIVQSID RVTQLVAGIS EASATQAAGI ASVNLAVADA ERATQENAAM AEQTAAAAAS LEAQAQALRQ AVAVFRLAGA APRSGGAGGQ LVALDQQRQV AVLDLLLDAG GGRGEVLRAN VAA //