ID A0A371SKX0_9BACI Unreviewed; 535 AA.
AC A0A371SKX0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 18-JUN-2025, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DZB84_05485 {ECO:0000313|EMBL:RFB18364.1};
OS Bacillus sp. HNG.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2293325 {ECO:0000313|EMBL:RFB18364.1, ECO:0000313|Proteomes:UP000263943};
RN [1] {ECO:0000313|EMBL:RFB18364.1, ECO:0000313|Proteomes:UP000263943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HNG {ECO:0000313|EMBL:RFB18364.1,
RC ECO:0000313|Proteomes:UP000263943};
RA Gagnon H.N., Maines B.A., Sevigny J.L.;
RT "Genome Assembly of Bacillus sp. HNG.";
RL Submitted (AUG-2018) 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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:RFB18364.1}.
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DR EMBL; QUQV01000002; RFB18364.1; -; Genomic_DNA.
DR RefSeq; WP_116351251.1; NZ_QUQV01000002.1.
DR AlphaFoldDB; A0A371SKX0; -.
DR OrthoDB; 9792686at2; -.
DR Proteomes; UP000263943; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:TreeGrafter.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR FunFam; 3.30.450.20:FF:000018; Sensor histidine kinase DcuS; 1.
DR Gene3D; 1.10.287.130; -; 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; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR039506; SPOB_a.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF3; SENSOR PROTEIN CITS; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF17203; sCache_3_2; 1.
DR Pfam; PF14689; SPOB_a; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 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:RFB18364.1};
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:UP000263943};
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 13..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 221..256
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 336..528
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 535 AA; 59573 MW; 6964C2746E199CA9 CRC64;
MLKLFNITLQ TKIITLILTL IVFVISVLTG MFLYYEAKDT NEEMQKLAIQ ASRTLSLIPI
MKDVSHEDVQ SGSMQAITQQ IGNQAGANYV LIEYKDGLNI SYPSYEVGHS AFDPENYKAI
VFGGYYTIET KNELGHILWG KAPIFAENNG QQIIGVASVG FLKNEIQQSM NHKLLKTLII
AIIVLIVGIL GGVLLAKSIR NDIMGLEPHE IASLFRERNA ILKSVKEGII AIDNKGFITL
LNNSAKQMLG ISNESINKPI AEILPNTRML RVLDSNMVES DDEMIINNRV LIVNRMPIIE
NGKTVGVVSS FRDKTEIKKM VDTLTEIKNY SEDLRAQTHE FTNKLYVLSG LLQLEQYEQA
IAMIQQETNQ LNFQNDILFN QIKDPKLQAI LLGKIGKASE KKVSLEIDEN SYLSELPIHI
SITDCIIIIG NLIDNAIDEV MQDEGIVTFF VTDIGNDIVF EVSDNGKGIP NDKISNLFEK
GISSKAEKNR GYGLWNVKTV VDKLNGSIEV ANGKNGGAIF SVFLPMKNQI DKEVD
//
