ID   A0A0P1GRR2_9RHOB        Unreviewed;       650 AA.
AC   A0A0P1GRR2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=TM5383_02594 {ECO:0000313|EMBL:CUH85365.1};
OS   Thalassovita mediterranea.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Thalassovita.
OX   NCBI_TaxID=340021 {ECO:0000313|EMBL:CUH85365.1, ECO:0000313|Proteomes:UP000051681};
RN   [1] {ECO:0000313|EMBL:CUH85365.1, ECO:0000313|Proteomes:UP000051681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8383 {ECO:0000313|EMBL:CUH85365.1,
RC   ECO:0000313|Proteomes:UP000051681};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CYSF01000012; CUH85365.1; -; Genomic_DNA.
DR   RefSeq; WP_058319420.1; NZ_FTNX01000003.1.
DR   AlphaFoldDB; A0A0P1GRR2; -.
DR   STRING; 340021.TM5383_02594; -.
DR   OrthoDB; 9796100at2; -.
DR   Proteomes; UP000051681; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 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; IPR035965; PAS-like_dom_sf.
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; PF12860; PAS_7; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000051681}.
FT   DOMAIN          319..525
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          534..647
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          598..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          148..185
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         584
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   650 AA;  71519 MW;  7C0C8F8837578E78 CRC64;
     MALGKNETAS MTNAGLNLIQ QGLSIFDDQL KMVLCNQRFR EMFDIPETYS SPGVHFEDTI
     RFLVERGEYG EVDDIEEAVK FRVDQARAFT PHYVERERSN GRWIAVEGSP LPQGGWVAVY
     TDITRTKRQE ALLRTRSEAL SDRVLGYAEE LAATNRELEA TVTALEEAKR QLAETEARTR
     QTTEMIPAHI AHVDRDRRYT FSNRKLSNVM PGRPSEITGL DIEEALGEEI YSEIAPHLDK
     AFAGEASVFE FFIESSSRRI RASFTPAQDL VRGTDGIHTS ADQNGGVYIL SMDITRESQA
     RTALQQTRRR ELAAQLASGM AHDFSNLLTI ILGSQSRLQR MDLPEQAQKQ VTATLSAAHR
     GGSLLNRIAD ITGAREWHPV PADVALLLDD MKILATPALP PGFTLHISNL LHEKMLMLDT
     GMLQDSLLNL ILNARDACGT SGEISLTVAP VQHLWAEFIV EDTGPGFSET ALERAMEPFY
     TTKGGEGSGL GLSMVYDTAK LAGGRLRIAN GEKGARITLR LPMRAARAAP KPGLVLLVED
     SSDIREVLRP MLTDMGNTVI EAASYDEARA LIDGVPGIAR ILSDISLVGE KTGLDLRDSL
     GPDAPPMHMM TSRPPTDPLH QAAARGGPVL RKPFTQSQLT SFLQQDPNIR
//