ID Q63EP4_BACCZ Unreviewed; 580 AA.
AC Q63EP4;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=yvrG {ECO:0000313|EMBL:AAU19230.1};
GN OrderedLocusNames=BCE33L1017 {ECO:0000313|EMBL:AAU19230.1};
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU19230.1, ECO:0000313|Proteomes:UP000002612};
RN [1] {ECO:0000313|Proteomes:UP000002612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L {ECO:0000313|Proteomes:UP000002612};
RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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; CP000001; AAU19230.1; -; Genomic_DNA.
DR RefSeq; WP_001010420.1; NZ_CP009968.1.
DR AlphaFoldDB; Q63EP4; -.
DR KEGG; bcz:BCE33L1017; -.
DR PATRIC; fig|288681.22.peg.4551; -.
DR Proteomes; UP000002612; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAU19230.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 362..580
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 580 AA; 66662 MW; 10FFBC3E7E6EFA85 CRC64;
MNFNKRLIIQ FILQHVFVLV TLLIAVVAAF TYLIFLVTST SYEPNIPDAD NFMIARYISS
EDGNISLKAE VKDLIKEKND WIQVVEENGK VLYHFNTPSD VPTSYTKASL FSYIQNHIEN
PYTFTYWEIE LEEKNVLVIY GGMLKSNALL KTIQKAHPSV STDSFTLTEE EQQLLSKEKA
TLQIFNSKGD EVFSYPNGKK KTFSVIQAAL NEREPWNHKE NTSSFYDTNS NHLLVVTAKN
EHYYPDDEID DVFTKKFLIG CGLILLIVFV YLVILSIWYG NKFGKPLLHA MRWLKNIAGG
KYEEPVSKKG KTIRFRKSGK EKWSFRLFSD VTNSLEHLSI TLKKNDAMRQ VLQQTREEWI
TGLTHDLKTP LSSIYGYALL LESKQYNWTD RDIQQFGSVM KEKSQYMTTL IDDLSLTYQL
KNNSLPAQHV NIEMNQFVQK VLLQFINNPT LQNQNIEFVP SSNKIQYFIE EKWFQRIIEN
LLVNAVKHNN ETTNVIVKLS QNATSFTLSI SDNGKGMDDK TKELLFERYY RGTNTEESNI
GTGLGLAITK QLVHAHNGAI SIDSELGKGT TIILVFPFRS
//
