ID   A0A3D9BXL3_9RHOB        Unreviewed;       638 AA.
AC   A0A3D9BXL3;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DRV84_03515 {ECO:0000313|EMBL:REC58111.1};
OS   Rhodosalinus sediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodosalinus.
OX   NCBI_TaxID=1940533 {ECO:0000313|EMBL:REC58111.1, ECO:0000313|Proteomes:UP000257131};
RN   [1] {ECO:0000313|EMBL:REC58111.1, ECO:0000313|Proteomes:UP000257131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WDN1C137 {ECO:0000313|EMBL:REC58111.1,
RC   ECO:0000313|Proteomes:UP000257131};
RX   PubMed=29043957; DOI=10.1099/ijsem.0.002424;
RA   Guo L.Y., Ling S.K., Li C.M., Chen G.J., Du Z.J.;
RT   "Rhodosalinus sediminis gen. nov., sp. nov., isolated from marine
RT   saltern.";
RL   Int. J. Syst. Evol. Microbiol. 67:5108-5113(2017).
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   -!- 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:REC58111.1}.
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DR   EMBL; QOHR01000003; REC58111.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D9BXL3; -.
DR   OrthoDB; 9796100at2; -.
DR   Proteomes; UP000257131; Unassembled WGS sequence.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd00075; HATPase; 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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08448; PAS_4; 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; 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; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257131}.
FT   DOMAIN          308..514
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          523..636
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          137..178
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         573
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   638 AA;  69010 MW;  90DACCE13AEBB560 CRC64;
     MAQRADRTQA LMTAGLNLIQ QALSIYDSDL RLAACNRRFQ EMFDLPGDLV APGARFEDTI
     RFLVRRGEYG AVADEEEAVR ARVEVARRFQ PHYMERTRAN GRTISVEGTP LPEGGWVSVY
     TDITPTKQHE ALLRARSEEL SDQLIAHAEE LAAANRELAA TNAALEEASR ELAAIEARTR
     LTAEMMPAHI AHVDEERRYT YSNRRLSSVM PGRPREIVGR PIAETLGRAA YARIAPHLDA
     AFAGRESVFE FTDEISARRI RVAFTPDRRE SGIEGVYILS MDVTEEAQAR AALQQTRRRE
     MAAQLTSGLA HDFSNLLTIV LGSQARLAEM TLPAEARPHI DATLAAARRG GTLLERLSQL
     TGARDWRPEP CATEDFLADL DVLARAALPG GVTLTIRNAL PGERLMLDPG LLQDALLNLI
     LNARDACGPE GRIGVTLSAL QGTWAEFAVT DTGPGFSDAA LHRGFEPFYT TKGAEGSGLG
     LAMVYDMAKL AGGRVVLGNT FSGARVALRL PLRTAPAEAA GRLVLLVEDS AEVRATIRDM
     LTELGHAVAE AASAAEARTL LETLPEIGAV LTDLTLEGEE TGLDLAESLG PGGPPVWIMT
     ALPADDPRHR AARARWPVLA KPFSAAHLAQ TLDAGRAA
//