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Database: UniProt
Entry: A0A101W9B5_9FIRM
LinkDB: A0A101W9B5_9FIRM
Original site: A0A101W9B5_9FIRM 
ID   A0A101W9B5_9FIRM        Unreviewed;       620 AA.
AC   A0A101W9B5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=APF77_14585 {ECO:0000313|EMBL:KUO68730.1};
OS   Clostridia bacterium BRH_c25.
OC   Bacteria; Bacillota; Clostridia.
OX   NCBI_TaxID=1734399 {ECO:0000313|EMBL:KUO68730.1, ECO:0000313|Proteomes:UP000057710};
RN   [1] {ECO:0000313|EMBL:KUO68730.1, ECO:0000313|Proteomes:UP000057710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c25 {ECO:0000313|EMBL:KUO68730.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) 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:KUO68730.1}.
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DR   EMBL; LOES01000238; KUO68730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101W9B5; -.
DR   STRING; 1734399.APF77_14585; -.
DR   Proteomes; UP000057710; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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; 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; 1.
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; IPR024478; HlyB_4HB_MCP.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF12729; 4HB_MCP_1; 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; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KUO68730.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
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..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          205..257
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          266..337
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          334..387
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          391..609
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   620 AA;  70367 MW;  7BD897C1970DD99B CRC64;
     MLKTLKGKIT LVYTCLVLMI AIIGSASVLN LYRLSKAIDG LMVDNYKSIN AISYMLEAFE
     RQDSATLIYI NVDIGKGIEL FTQNSNEFMK WYITASNNTT ETGEKELLNK VNKDYMDYSM
     LFSKLQEIRN KEGADESAYF YDTEMMPEFV KIKNELRELT HLNEVGMFSS KDEATKSTHE
     SMYVILALSA LAVTGGLLLS IHFTNRFMKP LDKLTTTIKS VKMGNWNQQI NVVSRDEIGE
     LSIEFNKLTK RLYQYEQSAL GKLMTEKNKS LAIVKSIPDP LIVLDTAYRI LLLNDTCEMF
     FGIEEKKVLK KHFLEAIRNE EIFEIVSNAF EDMVEMDDRI IKIEHKEEYY FNVIVTVIKD
     RESRVTGLII LLKDVTQLKQ LEKARTDFVS TISHEFKTPL TSIMMGTSMV LDGSMGTLNE
     EQQDVMNTIK EDGERLTRLV NDLLELSRIE SGSSAFDMEP CSIDTVIDNS VKQFAIQAAH
     KSVSISTRIE ENMPKVIADN EKITWVFNNL ISNALKYTNP GDEIVIDAFI ENGKMHVSVK
     DTGIGIPEEF QEKIFDKYVQ VRGQDLEARG TGLGLAVVKE IINTHGGEIW CESKMDTGSI
     FTFTLPLSFL EVPGEKNFGN
//
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