ID A0A1D7VWG1_9ACTN Unreviewed; 640 AA.
AC A0A1D7VWG1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SL103_08710 {ECO:0000313|EMBL:AOP51072.1};
OS Streptomyces lydicus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=47763 {ECO:0000313|EMBL:AOP51072.1, ECO:0000313|Proteomes:UP000094094};
RN [1] {ECO:0000313|EMBL:AOP51072.1, ECO:0000313|Proteomes:UP000094094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=103 {ECO:0000313|EMBL:AOP51072.1,
RC ECO:0000313|Proteomes:UP000094094};
RA Jia N., Ding M.-Z., Gao F., Yuan Y.-J.;
RT "Complete genome sequencing of Streptomyces lydicus 103 and metabolic
RT pathways analysis of antibiotic biosynthesis.";
RL Submitted (SEP-2016) 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};
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DR EMBL; CP017157; AOP51072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D7VWG1; -.
DR KEGG; slc:SL103_08710; -.
DR Proteomes; UP000094094; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 4.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 4.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AOP51072.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000094094};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AOP51072.1};
KW Transferase {ECO:0000313|EMBL:AOP51072.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..269
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 372..438
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 439..506
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 507..573
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 574..638
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 640 AA; 67738 MW; 225182AA92A8BD10 CRC64;
MLDGRYRVQA RIAAGGMATV YRAVDTRLDR VLALKVMHPG LAADGEFVDR FIREAKSVAR
LSHPNVVGVF DQGTDGTYVY LAMEYVAGCT LRDVLRERGA LQPRAALDIL EPILAALGAA
HRAGLVHRDM KPENVLIGDD GRVKVADFGL VRAVDTNTTS STGSVLGTVS YLAPEQLEHG
TADARVDVYA CGVVLYEMLT GSKPHTGGTV AQVLYQHLHE DVLPPSERVP GTAPQLDELV
ALATAREPEQ RAQDAVVLLS RARAARAELT DEQLDLVPPQ AKAVPAGDGS EPTDVIPRPA
GVQLPLPGAD EAELNRTSRL EVPPAEHTTR LRPAPAPAAP AGGLLQRRRL ATIVAAVLLV
LGVGTGVWYI NSGQFTSVPA VLDMPQAKAV STLRDAGLGV RVVRGFSSNV ERGHVMKTDP
ETGKRIRGTG TVTITVSRGP DIVAVPDLSG TPVADAKRKL RDRGLVPGTV TREFSTDVAK
GSVIRTDPKA GVKRRPDTAV ALTVSRGAPV DVPGVVGSDR ADAESTLRQA GFQVRFAEQP
VFSPEDKGTV ARQTPAEGGR LGKGDTVTLT LSKGPEMITV PDVTGKKVDD AKKELTSLGF
EVKVDKPWLF PQDEVDSQSV EGGQKAPKGG TITIKLKGAL
//
