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Database: UniProt
Entry: A0A068QW14_9GAMM
LinkDB: A0A068QW14_9GAMM
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ID   A0A068QW14_9GAMM        Unreviewed;       543 AA.
AC   A0A068QW14;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Methyl-accepting chemotaxis protein I {ECO:0000313|EMBL:CDG18070.1};
GN   Name=tsr {ECO:0000313|EMBL:CDG18070.1};
GN   ORFNames=XDD1_2371 {ECO:0000313|EMBL:CDG18070.1};
OS   Xenorhabdus doucetiae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG18070.1, ECO:0000313|Proteomes:UP000032721};
RN   [1] {ECO:0000313|EMBL:CDG18070.1, ECO:0000313|Proteomes:UP000032721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA   Genoscope - CEA;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FO704550; CDG18070.1; -; Genomic_DNA.
DR   RefSeq; WP_045971119.1; NZ_VNHN01000029.1.
DR   AlphaFoldDB; A0A068QW14; -.
DR   STRING; 351671.XDD1_2371; -.
DR   KEGG; xdo:XDD1_2371; -.
DR   HOGENOM; CLU_000445_107_16_6; -.
DR   OrthoDB; 9765776at2; -.
DR   Proteomes; UP000032721; 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   CDD; cd11386; MCP_signal; 1.
DR   CDD; cd19407; Tar_Tsr_sensor; 1.
DR   Gene3D; 1.20.120.30; Aspartate receptor, ligand-binding domain; 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   SMART; SM00319; TarH; 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   Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          214..266
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          271..500
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   543 AA;  59629 MW;  1BDA6E0BB85C5BC5 CRC64;
     MLGKLRISTS LYLLLMMFCV MQIISSGLSL GIIHTDQSYI ERIELGTQRR DTLGLSWAAL
     LQTRNTLNKI ALAQKVGQPQ TQIDEMEALL KSALNEAERN FAKLSALPRV EKSDQGIALF
     AEVEHAYQKY INALKELKTY LYEGNFQAFL DQPTEDYQRK METAYNNYMQ YLGANISSAV
     AEGEFYYKVA IAMFFGAVLM VFVVSGAAHW WLKRNLLRPF SNMRACFQDV AQGRLDKEVA
     VTTDDEIGDI FRKLRDMQTS LIKSIAAVRE NTNQMYSGIQ EISQGNTDLS SRTEQQAASL
     EETAASMEEL TVTVKQNAEN ARQASELAVS ASQTASKGGE LTTSVVVTMD EIARSSKKIG
     AIISVIDGIA FQTNILALNA AVEAARAGEQ GRGFSVVAGE VRDLAQRSAE AAKEIKTLID
     ESVQRVNQGS ELVNNAGQTM DELVRSVNQV TDLMAEIAAA SDEQSRGIHQ VAQAVSQMDQ
     VTQQNAALVE QSAAAASALE DKADMLVKTV AQFELPKDVE DEYDHPSSAA SNMTDEYVVS
     QVR
//
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