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Database: UniProt
Entry: F3FLY4_PSESX
LinkDB: F3FLY4_PSESX
Original site: F3FLY4_PSESX 
ID   F3FLY4_PSESX            Unreviewed;       543 AA.
AC   F3FLY4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Histidine kinase, HAMP region: chemotaxis sensory transducer {ECO:0000313|EMBL:EGH31220.1};
GN   ORFNames=PSYJA_20461 {ECO:0000313|EMBL:EGH31220.1};
OS   Pseudomonas syringae pv. japonica str. M301072.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=629262 {ECO:0000313|EMBL:EGH31220.1, ECO:0000313|Proteomes:UP000004471};
RN   [1] {ECO:0000313|EMBL:EGH31220.1, ECO:0000313|Proteomes:UP000004471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M301072PT {ECO:0000313|Proteomes:UP000004471};
RX   PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA   Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA   Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT   "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT   genomics of 19 Pseudomonas syringae isolates.";
RL   PLoS Pathog. 7:E1002132-e1002132(2011).
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGH31220.1}.
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DR   EMBL; AEAH01000932; EGH31220.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3FLY4; -.
DR   PATRIC; fig|629262.5.peg.3411; -.
DR   HOGENOM; CLU_000445_107_27_6; -.
DR   Proteomes; UP000004471; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; 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; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00304; HAMP; 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   Kinase {ECO:0000313|EMBL:EGH31220.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}; Transferase {ECO:0000313|EMBL:EGH31220.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        332..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          355..407
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          412..543
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   543 AA;  59089 MW;  1950FF30AE3684D0 CRC64;
     MNSLLSPGMR LMGHFGFARK FQVLFLLFML PLAGSAWVIT KEYSNKLDVI SGEQSGVRQL
     LALDDLNIEL SAQRDHAARW KAADILREPT PAAKAAMASV DAGIPRIAKA LEGVQAVLVE
     EKAPADTMNR FKALQAAVTG LDTASLRTVG WWPDGYDRFT TVLNLVQALR EQIAMDSGLI
     LDPWLETYML MQLSTQQVPD LIERIGRLSS VGQTSVASGQ FSLQSRLQMR DLRGRIDDSK
     DQMQKAAGLL LSKLPEQLQP WADKYAAVMQ VLEAQLKVID DGVFGGSIKL KPEEFEKSID
     TLTGSTTELR RQSLEALNGR LDYYHESSNT EFIPMALVFC VLVIMAIYLF ACLQSSIRNS
     ARGITTLAES LRDGNLCVEV AVQGRDELAA ISRALNVAVV QLRTSLLGVN QETVRVGDAV
     LTLNAQSSGT LSEVEDQQQQ ISQIAAAATE LAATSQGVAR SCEQASESAR QTRQIAQQSS
     QDSQRTTDSI QQLNQRLTET AAALGRVSEQ GQQIQSVVDA IRGIAEQTNL LALNAAIGGG
     ARR
//
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