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Database: UniProt
Entry: A0A291GAC0_9RHOB
LinkDB: A0A291GAC0_9RHOB
Original site: A0A291GAC0_9RHOB 
ID   A0A291GAC0_9RHOB        Unreviewed;       740 AA.
AC   A0A291GAC0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=CEW89_05780 {ECO:0000313|EMBL:ATG47125.1};
OS   Celeribacter ethanolicus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1758178 {ECO:0000313|EMBL:ATG47125.1, ECO:0000313|Proteomes:UP000217935};
RN   [1] {ECO:0000313|EMBL:ATG47125.1, ECO:0000313|Proteomes:UP000217935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSPH2 {ECO:0000313|EMBL:ATG47125.1,
RC   ECO:0000313|Proteomes:UP000217935};
RA   Woo J.-H., Kim H.-S.;
RT   "Celeribacter sp. TSPH2 complete genome sequence.";
RL   Submitted (JUN-2017) 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};
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DR   EMBL; CP022196; ATG47125.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291GAC0; -.
DR   STRING; 1758178.GCA_001550095_01320; -.
DR   KEGG; ceh:CEW89_05780; -.
DR   OrthoDB; 9764438at2; -.
DR   Proteomes; UP000217935; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; 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; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12860; PAS_7; 2.
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   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ATG47125.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000217935};
KW   Transferase {ECO:0000313|EMBL:ATG47125.1}.
FT   DOMAIN          384..597
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          621..737
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          71..98
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         672
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   740 AA;  81919 MW;  C5C466522A6E356D CRC64;
     MTRPSDFVLN PEDSPERSRE KLLKIVDVLM SQTEQRSNEH SAAYAQFQRA AMFEEQVRQR
     TVDLEYALDL LNVSNARLAE ANRDLDTARR NLANAIETVQ DGFALFDSDD VLVMYNSRFA
     SFLPDVRAAL HEGISFSNYA ELVGRSKHLD LTETDTAYAW AERRVERHKD RHVVFNIHVE
     GDRWVQISEH RTPDDGTVIL QTDVSDLVHA ERETRGRMLD DQAQMIHATL EHVSLGVCIF
     DKDARLAGFN QRLGYLMGLQ MSLMRIGARF DTMYQRTETA LTLSDGMTAE ALMAWVYGQA
     PRVPITFELK HVDHRVLVVS AEDLPDGGFV MSVTDVTAER RAMEELTRTN ETLEARVMSR
     TLDLEDALGR AERANAARSR FVAAASHDLL QPLSAAKLFV ASAEDDVTSP LAQETLAKAQ
     NALASVENIL SALLDISKLE AGRKALDIMP VPLAPMLMQL REEYLPAARA KGIDLRVVRT
     DKIVESDPTY LRRILQNLMS NAIRYTEEGR VLVGARRKPN GRVRLEVRDT GPGIPEASQQ
     AIFQEFHRLG TSASASVGMG LGLAIVDRAC AQLGHPIHLH SELGKGTVFG IDLAVTRHLA
     AQNITSFQAT PSAPDQAFGL IALLVENDAD VRRAMTLLLE KWGLAVVAVE NGEEALSLVA
     ELDVVPDLML VDYQLGEGID GIEVIRQMRG LYGAIPARLV TANRSPEVVQ HSAGAGVKIL
     YKPIAPQDLE RFVMAPQDEG
//
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