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Database: UniProt
Entry: A0A0U3PRJ1_9ACTN
LinkDB: A0A0U3PRJ1_9ACTN
Original site: A0A0U3PRJ1_9ACTN 
ID   A0A0U3PRJ1_9ACTN        Unreviewed;       319 AA.
AC   A0A0U3PRJ1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=AS200_04495 {ECO:0000313|EMBL:ALV31395.1};
OS   Streptomyces sp. CdTB01.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV31395.1, ECO:0000313|Proteomes:UP000068029};
RN   [1] {ECO:0000313|EMBL:ALV31395.1, ECO:0000313|Proteomes:UP000068029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CdTB01 {ECO:0000313|EMBL:ALV31395.1,
RC   ECO:0000313|Proteomes:UP000068029};
RA   Tian Y., Zhou G., Yang H., Lu X.;
RT   "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT   bacterium tolerant to cadmium.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SIMILARITY: Belongs to the anti-sigma-factor family.
CC       {ECO:0000256|ARBA:ARBA00037972}.
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DR   EMBL; CP013743; ALV31395.1; -; Genomic_DNA.
DR   RefSeq; WP_058921081.1; NZ_CP013743.1.
DR   AlphaFoldDB; A0A0U3PRJ1; -.
DR   STRING; 1725411.AS200_04495; -.
DR   KEGG; scx:AS200_04495; -.
DR   OrthoDB; 4088450at2; -.
DR   Proteomes; UP000068029; Chromosome.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   CDD; cd16936; HATPase_RsbW-like; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR025847; MEDS_domain.
DR   InterPro; IPR047718; RsbA-like_anti_sig.
DR   NCBIfam; NF041045; RsbA_anti_sig; 1.
DR   PANTHER; PTHR35526; ANTI-SIGMA-F FACTOR RSBW-RELATED; 1.
DR   PANTHER; PTHR35526:SF3; STAS DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13581; HATPase_c_2; 1.
DR   Pfam; PF14417; MEDS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068029};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          16..161
FT                   /note="MEDS"
FT                   /evidence="ECO:0000259|Pfam:PF14417"
FT   DOMAIN          202..311
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF13581"
SQ   SEQUENCE   319 AA;  35338 MW;  AC88FF57EFF6114F CRC64;
     MTSSPPLSTA PGTGYRHELY PYSGREEFVE GTASFIQDAL DGGEAVVVAV PHHKASLLRA
     EIREDEAVRY VDTSKVAHHP GRLIAAWQEW LQGHASDGRP VRGIGESPWE DVRSPAEAAE
     LRYHEWLLNK AFAQGPAWWL LCPYDVADSR AALREMARCH PELRRDGRTS PCEDYDPQAP
     YAFAPLNRPC DPHDEFAYGN GDLPALRDKI AACAELHGLA DRRLRELHLA ATEVAANSIR
     HGGGRGVLRL WSEDGRLVCE FRDAGYIADP LAGRIRPTAT QAGGRGLWLI HQLCDLVEIR
     STPAEGTTIR LHTELPERP
//
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