ID A0A0A8JMI9_BACSX Unreviewed; 683 AA.
AC A0A0A8JMI9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OXB_3509 {ECO:0000313|EMBL:BAQ11978.1};
OS Bacillus sp. (strain OxB-1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=98228 {ECO:0000313|EMBL:BAQ11978.1, ECO:0000313|Proteomes:UP000031651};
RN [1] {ECO:0000313|Proteomes:UP000031651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OxB-1 {ECO:0000313|Proteomes:UP000031651};
RA Yamaguchi T., Asano Y.;
RT "Complete genome of an aldoxime degrader Bacillus sp. OxB-1.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAQ11978.1, ECO:0000313|Proteomes:UP000031651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OxB-1 {ECO:0000313|EMBL:BAQ11978.1,
RC ECO:0000313|Proteomes:UP000031651};
RA Yamaguchi T., Asano Y.;
RT "Complete Genome Sequence of an Aldoxime Degrader, Bacillus sp. OxB-1.";
RL Genome Announc. 3:e00025-15(2015).
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; AP013294; BAQ11978.1; -; Genomic_DNA.
DR RefSeq; WP_052484139.1; NZ_AP013294.1.
DR AlphaFoldDB; A0A0A8JMI9; -.
DR STRING; 98228.OXB_3509; -.
DR KEGG; baco:OXB_3509; -.
DR HOGENOM; CLU_023032_0_0_9; -.
DR OrthoDB; 2485714at2; -.
DR Proteomes; UP000031651; 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 CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 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; 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; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAQ11978.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000031651};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 369..421
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 468..680
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 416..468
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 683 AA; 77775 MW; 9788F56B016C6A76 CRC64;
MLLLSLVPLI IISYFVIQST KNSITVTGAN IEEDISEYAL YLYKENINRQ AEATSIQLEG
YKKQILQLRT TLEEVFESSI VPPGYSLRLQ QDIGGVYWES VKGDFSNTGA TASYPVTAET
VERLEQTKSI EGTMKQIVKS NQAIVAVYYV SPTSAWRIYP AMNTPKEIHD GFLTADADFT
KETFYTAGAD VSPNSNKVGW TDPYIDLTHR HEMFSISAPI IGPNDEELGI LGADITTHRA
LNHLLNMKFK EEFAYALLLN QNDEFIAYQD QADNDLPFLT KAIRQQISLD EQPVLLNVNG
MNKIFLSATI DHTGWKLIFA IPEAGIVDHI KSLTDRQLAA HERTIFSHLR NVMIFTLLVI
ILCSIAIWRN FTKPIREILG GIRSFQNENF KAEIPSQSLH EFNLVSQSFN SMSQQINKLI
SNYQTLNSQL EDKVSERTQQ LVRLNISLIE TNKKLQETEQ QRKLLFANIA HDLKTPITLI
HGYIEAIQDG LIGEEDYERY FERIQNHLDS INNLVVNASE LNRIDLKEQP FHFQRVDTTS
FFQKLGTHFD QFKTVVFDIE PDLPSLDIDV HYIERAMMNL VKNALKYSEP DARIDVTVRQ
QDRHAIITVK DEGWGITKND LPYIFDRFYR VSKVRNSNKP GTGLGLSIVK EVITEHDGTI
VAHSEPGVGT EFTITLPFPM EED
//
