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Database: UniProt
Entry: E2QA76_STRCL
LinkDB: E2QA76_STRCL
Original site: E2QA76_STRCL 
ID   E2QA76_STRCL            Unreviewed;       571 AA.
AC   E2QA76;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SCLAV_4703 {ECO:0000313|EMBL:EFG09775.1};
OS   Streptomyces clavuligerus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1901 {ECO:0000313|EMBL:EFG09775.1, ECO:0000313|Proteomes:UP000002357};
RN   [1] {ECO:0000313|EMBL:EFG09775.1, ECO:0000313|Proteomes:UP000002357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC   NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357};
RX   PubMed=20624727; DOI=10.1093/gbe/evq013;
RA   Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA   Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA   Breitling R., Takano E.;
RT   "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT   evolutionary reservoir of secondary metabolic pathways.";
RL   Genome Biol. Evol. 2:212-224(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; CM000913; EFG09775.1; -; Genomic_DNA.
DR   RefSeq; WP_003962114.1; NZ_WMCC01000189.1.
DR   AlphaFoldDB; E2QA76; -.
DR   STRING; 1901.BB341_05390; -.
DR   GeneID; 61469229; -.
DR   KEGG; sclf:BB341_05390; -.
DR   eggNOG; COG3290; Bacteria.
DR   OrthoDB; 9792686at2; -.
DR   Proteomes; UP000002357; Chromosome.
DR   GO; GO:0005886; C:plasma 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; cd16915; HATPase_DpiB-CitA-like; 1.
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; 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   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF17203; sCache_3_2; 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFG09775.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002357};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFG09775.1};
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        20..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          223..263
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          424..535
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          536..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   571 AA;  60554 MW;  2EC50389160BE771 CRC64;
     MSPEPTAPPR RRRIGWPQRV FSQVLLMQLA IATGVTVLAT GFFLAPLSAQ LDDQAMRRAL
     AIAQTAASPQ VADGLATTRP TATGPVQTEA ERIRRTTGAE YVVIMDMTGV RWSHTSPEQI
     GRLVSTDPSA ALAGREVMEI DDGTLGRSAR GKVPLRDDAG RIIGAVSVGI EYDSVRDRLF
     SAIPGMLLYA GGALAAGAIA AYLISRRLQR QTHDLAFSDI SALLAEREAM LHGIREGVVA
     LDATGRIRLM NDEAQRLLGL ESDGRGLPLD EVLGAGRTAD VLAGRVTGED LLAVRGHRVL
     ITNRMPTDDG GAVATLRDRT ELERLGRELD STRGLIDALR AQDHEHANRM HTLLGLLELE
     MHDEAVSFVT EVVGVHRATA EQVTEKIHDP LLASLLVGKA TVAAERGVSL RIAPGTLLPD
     RVVDPRGLVT VLGNLVDNAM DAAAGSAEPG IEVELSSEGR TAVLRVADTG PGVPPEQREQ
     IFTEGWTTKE LPAHGKRGLG LALVRRLAER QGGSALVREA EGGGAEFVVV LPEALAPEAL
     TDGTPTDEGH EGSPDGTTAH EPKTATAAEA R
//
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