ID A0A1F6I5U4_9BACT Unreviewed; 438 AA.
AC A0A1F6I5U4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A3C22_01885 {ECO:0000313|EMBL:OGH18012.1};
OS Candidatus Levybacteria bacterium RIFCSPHIGHO2_02_FULL_37_10.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1798600 {ECO:0000313|EMBL:OGH18012.1, ECO:0000313|Proteomes:UP000178573};
RN [1] {ECO:0000313|EMBL:OGH18012.1, ECO:0000313|Proteomes:UP000178573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGH18012.1}.
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DR EMBL; MFNX01000007; OGH18012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6I5U4; -.
DR Proteomes; UP000178573; 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; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003018; GAF.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF32; DRUG SENSORY PROTEIN A; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 204..421
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 438 AA; 48640 MW; 7CA964725754ADBA CRC64;
MMQAPIPSNE KERLLSLHTL GLLDTNPEER FDRITRTATK IFHVPISTLT LVDERREWFK
SCQGLPNREG SRAISFCGHA LLANEIFVMP DTKKDIRFFD NPMVVGKPYI RFYAGVPIMN
ADGQRVGVFC IKDIEPRKFS KADGEILVGL AGWAELEVNS RNLSLALEER KEIEQKLIGE
KTKLKTANKK LESLDKLKDE FLSIASHELR TPLTAINGLV SMILGGEYGE VNANLREPLG
DVNASSERLI HLVNDLLSLS RIQAGKMMYT FSEFSIADAV NQAVHLLLPL SEQKGLRLTI
AKLEPVIIQG DSEKVKEVLN NLIGNSLKFT DKGSITISTK SEPDKINVYI TDTGIGITKD
DQNKLFGMFE QLESGKDKSA STGLGLHISR EMVRKMGGEL WIEKSETGIG STFAFSLPVA
KSKLAHEIKK AVDLTVKS
//
