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Database: UniProt
Entry: C0ZI45_BREBN
LinkDB: C0ZI45_BREBN
Original site: C0ZI45_BREBN 
ID   C0ZI45_BREBN            Unreviewed;       575 AA.
AC   C0ZI45;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=BBR47_43420 {ECO:0000313|EMBL:BAH45319.1};
OS   Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH45319.1, ECO:0000313|Proteomes:UP000001877};
RN   [1] {ECO:0000313|EMBL:BAH45319.1, ECO:0000313|Proteomes:UP000001877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47 / JCM 6285 / NBRC 100599
RC   {ECO:0000313|Proteomes:UP000001877};
RA   Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA   Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA   Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA   Udaka S., Tanikawa S., Fujita N.;
RT   "Brevibacillus brevis strain 47, complete genome.";
RL   Submitted (MAR-2005) 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}.
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DR   EMBL; AP008955; BAH45319.1; -; Genomic_DNA.
DR   RefSeq; WP_015892583.1; NC_012491.1.
DR   AlphaFoldDB; C0ZI45; -.
DR   STRING; 358681.BBR47_43420; -.
DR   KEGG; bbe:BBR47_43420; -.
DR   eggNOG; COG3275; Bacteria.
DR   HOGENOM; CLU_020473_3_3_9; -.
DR   Proteomes; UP000001877; 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   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   Gene3D; 1.10.1760.20; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR   Pfam; PF13492; GAF_3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 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:0000313|EMBL:BAH45319.1};
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:UP000001877};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAH45319.1};
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        44..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        103..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          460..565
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   575 AA;  63268 MW;  B329CED1B2C56515 CRC64;
     MNLALMVPLT ERTAVLIVMA LLFTRVRAFR SILNQQATWR EKALMVVIFS AISILGTYNG
     IWYQDAIANS RVIGTVVAGL LAGPWVGLMT GLIAGIHRYS LGGFTDLACA ISTISEGLFA
     GLIYQFLRNR SKKIGWTTAL FVGFLAEWLQ MGIVLLIARP YADALALVQA ISVPMSVVNS
     VGIAILIIII DLAKKEEDRI GALQAQRTLQ VADKTLSYLR QGLTYDSAQK VAEEILRTTR
     VAAVAITDTR SVLAHVGAGS SHHVVGEGIT TKATREVLST KEVKIAQTKE EIGCRETNCP
     LRYAILVPLM RRREVAGVLK LYQDRSRKLS AVDLELVRGL GNLISSQLEL AELEKQSRLL
     ADAEIRALHA QINPHFLFNA LNTIVSFIRF RPEQARELLI HLGEYFRRNL HDSGGYVSLA
     RELEHIEAYL AIERARFGDK LHVEYDIEDG VERFTVPGLI LQPLVENAVK HGLLPKREGG
     TVVIRACRKE KQIVELTVAD NGVGMEVDPS ERAPDEKRAG RQLSGIGLAN VKSRLQSIYG
     EPYGIVIESK SGSGTTCTIQ LPIGVNVSAQ SVHRR
//
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