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Database: UniProt
Entry: A0A3M8ANV5_9BACL
LinkDB: A0A3M8ANV5_9BACL
Original site: A0A3M8ANV5_9BACL 
ID   A0A3M8ANV5_9BACL        Unreviewed;       519 AA.
AC   A0A3M8ANV5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=EDM57_20660 {ECO:0000313|EMBL:RNB52872.1};
OS   Brevibacillus gelatini.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1655277 {ECO:0000313|EMBL:RNB52872.1, ECO:0000313|Proteomes:UP000268829};
RN   [1] {ECO:0000313|EMBL:RNB52872.1, ECO:0000313|Proteomes:UP000268829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100115 {ECO:0000313|EMBL:RNB52872.1,
RC   ECO:0000313|Proteomes:UP000268829};
RA   Dunlap C.;
RT   "Phylogenomics of Brevibacillus.";
RL   Submitted (OCT-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   -!- 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:RNB52872.1}.
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DR   EMBL; RHHS01000053; RNB52872.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8ANV5; -.
DR   OrthoDB; 9792686at2; -.
DR   Proteomes; UP000268829; Unassembled WGS sequence.
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; cd00130; PAS; 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; IPR003594; HATPase_C.
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; IPR033463; sCache_3.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR   InterPro; IPR039506; SPOB_a.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065:SF34; SPORULATION KINASE A; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF13596; PAS_10; 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   SMART; SM00091; PAS; 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   SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 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   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RNB52872.1};
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|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        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          321..516
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   519 AA;  58688 MW;  B987FF2369FB65DC CRC64;
     MLLSVGIVLF SLIIGMLIIV GGMIRVTENQ LGQRLMTIAR TVAQIPLVQE SIQEPDGWRQ
     INPTAHKLRV VNDVTYIVVL NMERVRYSDP LDERIGTVFA DPAVEEAYSE HSYLQKVKGD
     MGTALRAYVP IVDGQHQQVG VVLVGRVMPG TWEMMKNERG NIALTLFLSL LVGVWGSYLL
     ARHIKKQMLD LEPEQIARIL VERTATFHAM HEGVIAIDNQ ERITIFNDRA KQIFGIEGEV
     LGKPIRSVLP DTRLPEVLEL RQNFTNTELH VGNALLWSNR FLIKVEDKIV GALAIFQDRT
     EVARMAEELT GVKEFVGALR VQNHEHMNKL HTIAGLLQLN QYDKALAYLF EINEEQEELT
     SFLTTRIMDE NLSGLLIGKV SRGRELGIRV VIDRMSHLEK FPPYMDHHDF VLILGNLIEN
     AFDSLEQCER ADKEITISIE QDEEVCSILV EDNGIGMDEA TRAKMLERGF STKSRTDRGL
     GLHLVHQLVR KGRGELVCHS RPGEGASFMI TFPMKEVDE
//
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