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Database: UniProt
Entry: D7CEL1_STRBB
LinkDB: D7CEL1_STRBB
Original site: D7CEL1_STRBB 
ID   D7CEL1_STRBB            Unreviewed;       746 AA.
AC   D7CEL1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=SBI_05787 {ECO:0000313|EMBL:ADI08907.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI08907.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI08907.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI08907.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
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};
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DR   EMBL; CP002047; ADI08907.1; -; Genomic_DNA.
DR   RefSeq; WP_014178370.1; NC_016582.1.
DR   AlphaFoldDB; D7CEL1; -.
DR   STRING; 749414.SBI_05787; -.
DR   REBASE; 26503; SbiORF5788P.
DR   KEGG; sbh:SBI_05787; -.
DR   PATRIC; fig|749414.3.peg.5970; -.
DR   eggNOG; COG0323; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_012281_1_0_11; -.
DR   Proteomes; UP000000377; Chromosome.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
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   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ADI08907.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW   Transferase {ECO:0000313|EMBL:ADI08907.1}.
FT   DOMAIN          521..745
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   746 AA;  82316 MW;  E01C9138398B8201 CRC64;
     MDSENAKAYL RPRARLMSTL GEELISNERV ALTELVKNAY DADASLVLIR FNPPLEEGEG
     SIEVWDNGHG MSPATVSGTW MEIATPHRHR HPRSESGGRR VLGAKGIGRF ASARLAHTAA
     ITTRRVDEEE VTLRIDWGDF TEGDAYLDEV PVSLSTTSPT VFVDGGVASQ IFFEVLREFE
     TTPTTLDGAG HGTVVRLEKL RTAWGTDEIE TLKRSLSRLL PPPPPAELSV PDQPEFSIYI
     DTPEGPLRRH SGFVAASETL AHPRYRLVGT VDAGGNAHLA IYAGGEEPVE VVEDNLRKDS
     KRPSCGPLKL DFRVWDLESS AIKPLLALDT GAKNTNDVRE LIRNNSGVAL YRDGFRVQPF
     GEPGFDWLGF DQRRINNPTL RLSNRQVAGF VYISADDNPG LLDRSHREGL IDTPEYDELK
     AVILQAIARL ETQRYRLRRE PTAPMESPLL TDQPDGRGHG LFQNFNLDPL RQVAAERHPD
     DVILSRAIEE ATETINEGVR KVQEIIAQFS RLATLGTLVD VVLHDGRTAL SRIGVGLRRL
     GKITTKVEVH DAELSTALGK LQTDFTTQER ALDRLFARIE PLSGRKRGRP RRLSLHQSIA
     EAVDVLESEI TKHGVEVKIG GEDVIVTAEP GDIRTLVVNL VSNAVYWLST MPKGTPREIL
     IETERNHEGE LDVVDITVSD NGPGVREEIQ DLIFETYFSD KPDGVGLGLS IAGSVVKDFY
     DGDLGLVSPG TLLGASFRAR LRRRVG
//
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