ID A0A0Q9PWA9_9ACTN Unreviewed; 713 AA.
AC A0A0Q9PWA9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=ASG76_17965 {ECO:0000313|EMBL:KRE92328.1};
OS Nocardioides sp. Soil774.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736408 {ECO:0000313|EMBL:KRE92328.1, ECO:0000313|Proteomes:UP000051100};
RN [1] {ECO:0000313|EMBL:KRE92328.1, ECO:0000313|Proteomes:UP000051100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil774 {ECO:0000313|EMBL:KRE92328.1,
RC ECO:0000313|Proteomes:UP000051100};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE92328.1, ECO:0000313|Proteomes:UP000051100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil774 {ECO:0000313|EMBL:KRE92328.1,
RC ECO:0000313|Proteomes:UP000051100};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRE92328.1}.
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DR EMBL; LMSM01000012; KRE92328.1; -; Genomic_DNA.
DR RefSeq; WP_056607149.1; NZ_LMSM01000012.1.
DR AlphaFoldDB; A0A0Q9PWA9; -.
DR STRING; 1736408.ASG76_17965; -.
DR Proteomes; UP000051100; Unassembled WGS sequence.
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-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 3.
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; IPR030616; Aur-like.
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; PTHR24350; SERINE/THREONINE-PROTEIN KINASE IAL-RELATED; 1.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRE92328.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 425..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..294
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 446..513
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 514..581
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 582..648
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 649..713
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 305..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 713 AA; 74821 MW; 87F4EFBC4B3D7346 CRC64;
MEPPEHARAA APGAAGDPLV GRLLDGRYRI GSRVARGGMA SVYEATDTRL DRTVAVKVMH
PGLGDDQEFA ERFVREARAA ARLNHPHVVG VYDQGDDTSD GQDTVFLVME YVPGHTLRDV
IRKEAPMPPA RALALLEPVV SALAAAHRSG LIHRDVKPEN VLIADEAHGG RVKVADFGLA
KAVSADTQHT ATGGVLIGTV SYLAPELVVD GRADARADVY AAGVVLFELL TGRKPHEGES
PIQVAYRHVH HDVPMPSTLR PDIPDYVDAL VARATSRDRG QRAADAGVLL HQLHRVEQAL
REGLASDPEL SADLLPRRTP VSDEAAGPDD TTPEPFDAGA LALLTEVDPR DSGLVDDGSP
DRTTALERHP VAAAPTAIPA PLTEPMTTVA PGTRETDRPT APSRAPSRPA PVATAGRHRS
VKGPLALALA ILLVAGIGVG AYWFGWERYT TTPGVLGLDE AAATAELQDA GLEAEAGEGA
YSESVAAGLV VATDPGPGGK VLDGGTVTLV LSLGPERYDV PDLAGRTEDE AQDALAATRL
DFGESKGRWS ETVPEGQVIR TSPKAGTTLK PGAVVDLVLS RGRKPIEVKD FTGKSFADAR
EALEARGLEA TVASQVYSDT VPEGVVISQD PTTGTLFRGD AVSFVVSRGP ELVEVPRVEA
MGIEAATELL EGLGFTVKTK QAEIYLGLGY VSSSDPGEGE RVAKGSTITL SVV
//
