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Database: UniProt
Entry: A0A316IGR1_9GAMM
LinkDB: A0A316IGR1_9GAMM
Original site: A0A316IGR1_9GAMM 
ID   A0A316IGR1_9GAMM        Unreviewed;       877 AA.
AC   A0A316IGR1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=C7456_10159 {ECO:0000313|EMBL:PWK92727.1};
OS   Fulvimonas soli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Fulvimonas.
OX   NCBI_TaxID=155197 {ECO:0000313|EMBL:PWK92727.1, ECO:0000313|Proteomes:UP000245812};
RN   [1] {ECO:0000313|EMBL:PWK92727.1, ECO:0000313|Proteomes:UP000245812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14263 {ECO:0000313|EMBL:PWK92727.1,
RC   ECO:0000313|Proteomes:UP000245812};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:PWK92727.1}.
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DR   EMBL; QGHC01000001; PWK92727.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316IGR1; -.
DR   OrthoDB; 9764438at2; -.
DR   Proteomes; UP000245812; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd12914; PDC1_DGC_like; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.250.3020; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR033479; dCache_1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12860; PAS_7; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000313|EMBL:PWK92727.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000245812};
KW   Transferase {ECO:0000313|EMBL:PWK92727.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          521..734
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          758..873
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         808
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   877 AA;  95937 MW;  395F1512DB8A9BAE CRC64;
     MTRRHRRLTA VLLLAAAMLA SAWGAGRIAQ ERALRRLSAQ AAGQLQLRAL ALQRFVDRYR
     VLPTVLALDP VLRQALEAPA GRVDTAALNR KLEQANGLTH VSTLTLIDRR GVALAASNWR
     EPSSNVGLDY GFRPYFQLAM AHDHGSFYGI GVSTNVAGYF IAEAVHDADG RRIGVVVVKI
     TLDTVEREWA GDPATILLSD AHGVVFLSNR PAWLYHPLQP LAPAAAQALH ATRQYGEQPL
     RPIRARTVAR LADGGRRVRV TQPPLAHEVL WQSIALPSQG WTAHLLVDTR EAAHAGWRAA
     LVVLGGWLPA ILLGLFLQQR LRVARLRQRS REELERLVAH YAGALRSTQD SLVQAALQAA
     AGDPDCLERL PQGVSVVDKQ LRLVAWNRRY AELMQYPSGL LRKGRPVEDL FRHNAQRGLL
     GPGDVEEAIQ RRLDYLREGG PHTYERERPD GSVLEIRGHP LPDGGFVTSY ADITAYKDAA
     RELRTLTATL ESRIDAATRE QRLATAAAHR ANRDKTRYVA AAVHDLLQPL NAARLFAGAL
     REPLHGAGGR ALLARVEHAL QALESQLTSM LDLARLDAGG FKTQVADVPL SPLLGELARQ
     FGIVAQARGL RLDFVDTRAW VRSDPVLLRR ALQNFLSNAV HYTPRGRVLL GCRRDGDQLR
     IEVWDTGVGI PDDQRELIFQ EFRRLDSGVD ADERSAGLGL SIVRRIAQLL GHDVSVRSWP
     GGGSVFAIRV PRAAPAEAGE APGAAPAADT DSPLVGRRIL CIDDDTQART AMTVLLRRWG
     CRVDTAGDAI EAAMLAGSAP APDLVLLDYQ LGDTTGPALL PDLHRRWGCE PPVIVLTARN
     DAGVRAELET AGLRFMLKPV SPSRLRALMS RLLAHHG
//
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