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Database: UniProt
Entry: A0A150N0B1_9BACI
LinkDB: A0A150N0B1_9BACI
Original site: A0A150N0B1_9BACI 
ID   A0A150N0B1_9BACI        Unreviewed;       542 AA.
AC   A0A150N0B1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=B4110_1620 {ECO:0000313|EMBL:KYD30111.1};
OS   Parageobacillus toebii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX   NCBI_TaxID=153151 {ECO:0000313|EMBL:KYD30111.1, ECO:0000313|Proteomes:UP000075324};
RN   [1] {ECO:0000313|EMBL:KYD30111.1, ECO:0000313|Proteomes:UP000075324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4110 {ECO:0000313|EMBL:KYD30111.1,
RC   ECO:0000313|Proteomes:UP000075324};
RA   Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA   Eijlander R.T., Kuipers O.P.;
RT   "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT   Foods.";
RL   Submitted (JAN-2016) 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}.
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:KYD30111.1}.
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DR   EMBL; LQYW01000058; KYD30111.1; -; Genomic_DNA.
DR   RefSeq; WP_062678066.1; NZ_LQYW01000058.1.
DR   AlphaFoldDB; A0A150N0B1; -.
DR   PATRIC; fig|153151.4.peg.3278; -.
DR   Proteomes; UP000075324; 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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd16915; HATPase_DpiB-CitA-like; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd18773; PDC1_HK_sensor; 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; 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; IPR016120; Sig_transdc_His_kin_SpoOB.
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   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.
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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, 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        169..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          206..246
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          331..526
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   542 AA;  60550 MW;  92D3C4EBDB33B341 CRC64;
     MKLQTRLIII ICSLLLFVIV FLSFLFQHMF AATLKEQIGM RALNVAETVA ATPLVRDAFR
     QPDPHRQIQP FAEMIRRKTG AEYVVVGNRQ GIRYAHPLPD RIGKKMVGGD NDEVLEGKAI
     ISEAVGSLGP AIRGKAPIFD EKGNVIGIVS VGFLLEDIED IVWSYNAKIF FFSILALLLG
     VIGAVAIAKA VKKSIHGLEP KEIGMLYQEK QAILEAIREG IIAVNREGII TMVNKTAMEL
     LGYKKEYDVL GKYILHIIPY SRLLEVIRTG KAEYDDETIL GGETVIANRI PIVDKKGNVI
     GAVSTFRNKS ELYRLTKELS QLKSYADALR AQTHEFSNKL YVISGLIQLE SYEEALELIS
     KETNLHQDIV RFVMKEIPDP VIGGLFIGKF NRANELKIQF EIDRQSSFKD IPKHLDRDHL
     LTIIGNIVDN AMEAVLHNGC EEKRVTVFLT DLGDDLIIEV EDNGPGIQAE IADQIFERGF
     STKAAAHRGY GLDLVKKSLT VLGGHITYQS EQGKGTVFTI IIPKQRRVDD GLQYSSAHCR
     RR
//
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