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Database: UniProt
Entry: Q4LBM3_PSESH
LinkDB: Q4LBM3_PSESH
Original site: Q4LBM3_PSESH 
ID   Q4LBM3_PSESH            Unreviewed;       637 AA.
AC   Q4LBM3;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:CAI36075.1};
GN   Name=pph34 {ECO:0000313|EMBL:CAI36075.1};
OS   Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv.
OS   phaseolicola).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=319 {ECO:0000313|EMBL:CAI36075.1};
RN   [1] {ECO:0000313|EMBL:CAI36075.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1302A {ECO:0000313|EMBL:CAI36075.1};
RX   PubMed=16360685; DOI=10.1016/j.cub.2005.10.074;
RA   Pitman A.R., Jackson R.W., Mansfield J.W., Kaitell V., Thwaites R.,
RA   Arnold D.L.;
RT   "Exposure to host resistance mechanisms drives evolution of bacterial
RT   virulence in plants.";
RL   Curr. Biol. 15:2230-2235(2005).
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; AJ870974; CAI36075.1; -; Genomic_DNA.
DR   RefSeq; WP_054072882.1; NZ_LGKY01000010.1.
DR   AlphaFoldDB; Q4LBM3; -.
DR   PATRIC; fig|319.14.peg.3720; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 1.20.1440.210; -; 2.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR032255; HBM.
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; PF00672; HAMP; 1.
DR   Pfam; PF16591; HBM; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM01358; HBM; 1.
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.
DR   PROSITE; PS51753; HBM; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
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        288..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          45..281
FT                   /note="HBM"
FT                   /evidence="ECO:0000259|PROSITE:PS51753"
FT   DOMAIN          308..360
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          365..601
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   637 AA;  69142 MW;  88BFDFD449269D01 CRC64;
     MSNTKSGLLS NMTVRAKLLL GFSLLICIVL SMAYTGWKAT EFLKDRSERI GDISLFSSIA
     RDMRIERLVY FLKADDAQAS KWMEALERTE LQLKAITPRF NSAVNVALLR EADATMQRYR
     SFYEQAVRAT RDREKLRIVA AASAEAANNL LIKIADSANS ETGKFEERQK LTLLFVSVQK
     MRTSFRAYTA SPNASAEDTV RRAIGEVITQ TDVFKNVSTS AAIVQNLARV FADYGKQLEA
     LVAVQAKVDE AQAGITSSIT KILDISDKMT AIQNEFRVSD ASDAQNKIML WLILSIISGV
     LAAWLITRSI VQPLKETVAI VQIVAGGDFT YNASVTRKDE LGALQSSMLH MTSRLRNLIG
     EMKDGVVQVA SSAEELSAVT EQTSAGVNAQ KLETEQIATA MQQMTATTHE VSRNAAHAVN
     TAQNSSSLAV KGGQVVDKTR VQIESLAREM DTTKTAMAAL RGNAQSIGGV LDVIKAVADQ
     TNLLALNAAI EAARAGEAGR GFAVVADEVR GLAVRTRTST DEIAVLISEL QVSTDHMTQV
     LEQNLLLTDS SVDLSRQASE MLQSITTSVH EIELMNEQIA VATEEQNNVG EEIGKGVTNV
     RNISDQTAAA SEETATSSIE LARVSARLQE MTSRFTV
//
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