ID B1VND7_STRGG Unreviewed; 818 AA.
AC B1VND7;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE SubName: Full=Putative molecular chaperone with protein kinase domain {ECO:0000313|EMBL:BAG16960.1};
GN OrderedLocusNames=SGR_131 {ECO:0000313|EMBL:BAG16960.1};
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG16960.1, ECO:0000313|Proteomes:UP000001685};
RN [1] {ECO:0000313|EMBL:BAG16960.1, ECO:0000313|Proteomes:UP000001685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX PubMed=18375553; DOI=10.1128/JB.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
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 heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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DR EMBL; AP009493; BAG16960.1; -; Genomic_DNA.
DR AlphaFoldDB; B1VND7; -.
DR KEGG; sgr:SGR_131; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_345427_0_0_11; -.
DR Proteomes; UP000001685; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 2.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:BAG16960.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:BAG16960.1}.
FT DOMAIN 15..274
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 294..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 818 AA; 86071 MW; 28CB3C4D1712269C CRC64;
MEPLRAGDPE SVGGFVLRGR LGAGGMGEVF LGRSPGGRAV AVKVVHPHLA RQEEFRQRFA
REVAAARAVS GAFTAPVMAA GPEDDRPWIA TVYVPGPDLA TAVGVAGPLP EGAVWRLAAG
LVEALQAIHV VGVVHRDLKP SNVLVAADGP RVIDFGIART LEDTPLTMTG LVVGTAGFMA
PEQAEGGKVG SACDVFALGA VIAFAATGAG PFGEGPQLAV LRRVVGGRPR LDGLTGPLRE
LVEACLAKDP RDRPALATLL ERIGAHWEPA DEFRGGSPWP EAVTTLIQRH ATPPTAPYTE
AAGATAPPDG GPNAARRARR AVGIDFGTTN SAVAVMEGGE VLLIPNAQGR HTTPSLVALT
AEGDALVGTD AERQALANPG FTAGAAMLWL GTDWRVARGG VRLTAEDVAG LVLARLREDA
EAYLGEPVTD AVLAVPAGFR RDQRAALVAA GERAGLNVLR LVNVPTAVAT SYGPNRDDLT
VLVFDLGGGT LDVSLIELGD GVVEIRATAG DSRLGGNDWD QRIVEHLTDH VRRRHGVDLT
GDVAAIQRLR EAAETARIEL SAARTTTVRL PYLATGPDSP VHLEEELTRE ELERLTQDLL
ERCRTPVENV LADAGCTLAD IDQVVLTGGA ALMPAVGDLV RRLTGGQGSY QRLSPEAVVH
GAVLQAGILT GEVKDVLLLD VAPYSIGVET HDGTMKKLLQ RNTTIPTRRS DVFTTHTDDQ
PMVLFHIVEG ERKDAARNWP LAVLELALPP APRGVPMIEV TVDCTASDDL HIKVRDLGTG
NETSATVGQA TKERAAALLR SSRWARLRDL VPVTHPAC
//
