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Database: UniProt
Entry: F3CHL0_PSESG
LinkDB: F3CHL0_PSESG
Original site: F3CHL0_PSESG 
ID   F3CHL0_PSESG            Unreviewed;        52 AA.
AC   F3CHL0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Histidine kinase, HAMP region: chemotaxis sensory transducer {ECO:0000313|EMBL:EGH18752.1};
DE   Flags: Fragment;
GN   ORFNames=Pgy4_37916 {ECO:0000313|EMBL:EGH18752.1};
OS   Pseudomonas savastanoi pv. glycinea str. race 4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=875330 {ECO:0000313|EMBL:EGH18752.1, ECO:0000313|Proteomes:UP000005466};
RN   [1] {ECO:0000313|EMBL:EGH18752.1, ECO:0000313|Proteomes:UP000005466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000005466};
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:EGH18752.1}.
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DR   EMBL; ADWY01003119; EGH18752.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3CHL0; -.
DR   HOGENOM; CLU_215112_0_0_6; -.
DR   Proteomes; UP000005466; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR32089:SF112; METHYL-ACCEPTING CHEMOTAXIS PROTEIN CTPH; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:EGH18752.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}; Transferase {ECO:0000313|EMBL:EGH18752.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          1..52
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   NON_TER         52
FT                   /evidence="ECO:0000313|EMBL:EGH18752.1"
SQ   SEQUENCE   52 AA;  5414 MW;  1CA94E7B495A24B2 CRC64;
     MVNEAIAQIE RLASAVGNSS EAMGALKQES DKIGSVLDVI KSVAEQTNLL AL
//
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