ID C6XR81_HIRBI Unreviewed; 954 AA.
AC C6XR81;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Hbal_2943 {ECO:0000313|EMBL:ACT60612.1};
OS Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hirschia.
OX NCBI_TaxID=582402 {ECO:0000313|EMBL:ACT60612.1, ECO:0000313|Proteomes:UP000002745};
RN [1] {ECO:0000313|Proteomes:UP000002745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418
RC {ECO:0000313|Proteomes:UP000002745};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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; CP001678; ACT60612.1; -; Genomic_DNA.
DR RefSeq; WP_015828762.1; NC_012982.1.
DR AlphaFoldDB; C6XR81; -.
DR STRING; 582402.Hbal_2943; -.
DR KEGG; hba:Hbal_2943; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_308995_0_0_5; -.
DR OrthoDB; 9795133at2; -.
DR Proteomes; UP000002745; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR029016; GAF-like_dom_sf.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-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; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ACT60612.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002745};
KW Transferase {ECO:0000313|EMBL:ACT60612.1}.
FT DOMAIN 191..234
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 601..645
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 743..954
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 584..611
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 954 AA; 107354 MW; 345E859C4203C748 CRC64;
MTGSETDFKS RQQFELDRFD ELWKAAYLVV EDPQSTVVNR SDEFVKGLLK LAYSIFQVEM
IGLRCAQTGD EFILHQGAFK KHQRDPAIGN AYWSEFNNKP EGCILSDFKE KRSANNEILL
NISQKANYFA CFPLKAYGDV EAHFFLAHSS EIQFKEAEIF QIKSIIDLLE NMVSTCPEVL
NSEKFALVRM EMARLKAIVE SISGEVFILD TTQRGVIVAN ALVCKKLGYT RQELKSLTFL
ELCSIGPDEL DRHISLLDSH DGQKITFETA FIRKDHSIYP VNVELTLDKN GQKPVLVIFA
QDVSEHQNYP TQLEVMSAHH RSALAANMEM GFCVDVVFSP IGEFEDLIVK YADLGRYAFP
GFSELDMMGQ RVLATFPDVG KTGLVEKILP ALDMDELLVF DHHYISPNFE EWFRVSVLKD
GEKSLQIGLR GISDKKRRER ALMELYELSA DLDISTDEYL KKMLLAGRTA LGMEYAFVCA
IEGDNVRMEC SSKDNDCAHE LTYFPFEKTI LSRIWPLDKA VFLSDIDLVS NLYEGEDISV
RAYAAAPIFV QGDVVSFVSF ISEQANKTEY DEFQIGIISV IARMISQRKT LDLAREELEK
SRDELQLIFD NVPTSIWRKD RNHRYLKVNK SAADLVGMSV KDIVGLRPQD VFVNFDEKAC
LALDEQVLAT GKAMLGVEVE GGLGPDTWES IDIIPVLGEG VENEGWLIIS TDITRQKHAE
MKLAVVVDEL EAANKNLEQF NTVVSHDLKA PLRHMRMLSE LLSLSVQPDS EAAEYAALIQ
ENAVHGQAMV DSLNALSRVS RSELKRVPTD LRKTISMIEA LLSDELEEVG GRIVVNPLPS
IDVDAELVLN LFQNLIENSM KYRSDASPVI TIGVDTESKV PVFFVQDNGL GIKPDYSQEI
FQIFTRVHES ASPPKGDGVG LSICRRIIER HGGKIWLDED YTGGARFKFT FAAS
//