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Database: UniProt
Entry: U5LHR0_9BACI
LinkDB: U5LHR0_9BACI
Original site: U5LHR0_9BACI 
ID   U5LHR0_9BACI            Unreviewed;       609 AA.
AC   U5LHR0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=N288_25840 {ECO:0000313|EMBL:AGX06998.1};
OS   Bacillus infantis NRRL B-14911.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1367477 {ECO:0000313|EMBL:AGX06998.1, ECO:0000313|Proteomes:UP000017805};
RN   [1] {ECO:0000313|EMBL:AGX06998.1, ECO:0000313|Proteomes:UP000017805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-14911 {ECO:0000313|EMBL:AGX06998.1,
RC   ECO:0000313|Proteomes:UP000017805};
RA   Massilamany C., Smith T.P.L., Loy J.D., Barletta R., Reddy J.;
RT   "Complete genome sequence of Bacillus infantis NRRL B-14911 that has
RT   potential to induce cardiac disease by antigenic mimicry.";
RL   Submitted (JUL-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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP006643; AGX06998.1; -; Genomic_DNA.
DR   RefSeq; WP_009794702.1; NC_022524.1.
DR   AlphaFoldDB; U5LHR0; -.
DR   STRING; 1367477.N288_25840; -.
DR   GeneID; 85554736; -.
DR   KEGG; bif:N288_25840; -.
DR   PATRIC; fig|1367477.3.peg.5159; -.
DR   HOGENOM; CLU_000445_89_2_9; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000017805; Chromosome.
DR   GO; GO:0005886; C:plasma 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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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; IPR003660; HAMP_dom.
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; IPR013767; PAS_fold.
DR   InterPro; IPR049814; Resp_reg_WalK.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; NF033092; HK_WalK; 1.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AGX06998.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017805};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          206..258
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          263..326
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          385..602
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   609 AA;  69059 MW;  ED5B2580B0955F59 CRC64;
     MKKVGFFRSI HLKFVLIYVL LIIIAMQIIG VYFVGQLEKT LRSNFQTAIE ERVDLLSVYL
     EEIITKERPA GEDLPTKEEE VQRILRDYTS KDIIELRVID GETQKVLGSN KDGYVNQKAV
     DALTTSALAT RAPKSDEYTD QSLGNRRVWV LASPVKSANE EVVGVVYVKA DIENVFEQKN
     QINSIFASGI IIALAITALL GILLAQTITR PLSDMRRQAL AMAKGNFSRK VKVYGYDEIG
     QLAITFNSLT KKLQEAQATT EGERRKLSSV LSYMTDGVIA TDRRGRVILI NEPAAKMLNV
     PRETVLSSPI VNLLGLEEDY TFEELLAERE SVILDYSTET TPYVLRANFS VIQKETGFVN
     GLITVLHDIT EQEKIDLERR EFVANVSHEL RTPLTTMRSY LEALAEGAMH DEDIAPQFLN
     VTRTETERMI RMVNDLLQLS KLDSKDYRMK KEWVNFVDFF NRIIDRFDFS KEQNVTFQRN
     LPEHAAFVEI DEDKLTQVVD NIISNALKYS PEGGQVSFNI VEQEEQLLIR ISDQGVGIPK
     DNLDKVFERF YRVDKARTRK LGGTGLGLAI AKEVVEAHDG KIWAESTEGK GTTISFTLPF
     VRSDEDDWE
//
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