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Database: UniProt
Entry: U4V431_9RHOB
LinkDB: U4V431_9RHOB
Original site: U4V431_9RHOB 
ID   U4V431_9RHOB            Unreviewed;       357 AA.
AC   U4V431;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=HIMB11_01997 {ECO:0000313|EMBL:ERL97470.1};
OS   Rhodobacteraceae bacterium HIMB11.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1366046 {ECO:0000313|EMBL:ERL97470.1, ECO:0000313|Proteomes:UP000016848};
RN   [1] {ECO:0000313|EMBL:ERL97470.1, ECO:0000313|Proteomes:UP000016848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HIMB11 {ECO:0000313|EMBL:ERL97470.1,
RC   ECO:0000313|Proteomes:UP000016848};
RA   Durham B.P., DeLong E.F., Rappe M.S.;
RT   "Draft genome sequence of marine alphaproteobacterial strain HIMB11, the
RT   first cultivated representative of a unique lineage within the Roseobacter
RT   clade possessing a remarkably small genome.";
RL   Submitted (AUG-2013) 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   -!- 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:ERL97470.1}.
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DR   EMBL; AVDB01000006; ERL97470.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4V431; -.
DR   STRING; 1366046.HIMB11_01997; -.
DR   PATRIC; fig|1366046.3.peg.2024; -.
DR   eggNOG; COG5002; Bacteria.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000016848; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ERL97470.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016848};
KW   Transferase {ECO:0000313|EMBL:ERL97470.1}.
FT   DOMAIN          121..347
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   357 AA;  39821 MW;  DA4110E73759A0AF CRC64;
     MENEQIISIV SGLPYPCVAI SMRDFERILC ANPEAKAFLG DGIEGRHFYT VFRQPTMIEA
     IEGAIKSGER KNARVTISEN RRDAFYDATC INIAGQYCLV TFQDRSDQEQ IQQMRRDFVA
     NVSHELKSPL AALMGFIETL RTVAKDDLKA QERFLGIMES EAQRMNRLVN DLLSLSQVEA
     TARQRPTENI DLHGLIEQTV DILLPAAKAR DVVVNFVKQA NTVITVKGDS DQLHQVFNNL
     IENAIKYGAQ GGNVTVTLSQ PGYLPALRSE GIEVTVSDDG PGIDPVHLPR LAERFYRIDS
     HRSRQMGGTG LGLAIVKHII SRHRGRLMVD SVMGQGSNFR VLLPYDISIR AKRNDVS
//
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