ID A0A2N3XX25_SACSN Unreviewed; 661 AA.
AC A0A2N3XX25;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=A8926_2868 {ECO:0000313|EMBL:PKW15180.1};
OS Saccharopolyspora spinosa.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=60894 {ECO:0000313|EMBL:PKW15180.1, ECO:0000313|Proteomes:UP000233786};
RN [1] {ECO:0000313|EMBL:PKW15180.1, ECO:0000313|Proteomes:UP000233786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44228 {ECO:0000313|EMBL:PKW15180.1,
RC ECO:0000313|Proteomes:UP000233786};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 Actinobacteria strains.";
RL Submitted (DEC-2017) 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:PKW15180.1}.
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DR EMBL; PJNB01000001; PKW15180.1; -; Genomic_DNA.
DR RefSeq; WP_029535278.1; NZ_PJNB01000001.1.
DR AlphaFoldDB; A0A2N3XX25; -.
DR STRING; 994479.GCA_000194155_02573; -.
DR Proteomes; UP000233786; 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; 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; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:PKW15180.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:PKW15180.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 372..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..285
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 395..461
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 462..530
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 531..600
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 298..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..330
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 70222 MW; 913FD669B91F0937 CRC64;
MTPETRSSGA SLVGAMLERR YRVDSLIARG GMSTVYRGLD TRLDRPVAIK VMDAQYSGDR
SFVERFEREA RAAARLHHPD IVAVYDQGVD HGPAGDHVFL VMQLVEGCTL RDLIMDCGGR
LPLPTALSVM APVLSALGAA HQADMVHRDV KPENVLIGTD GSVMVADFGL VRAAAEAGTT
SGGVILGTVA YLSPEQVTTG AADARSDVYA AGIVFYEMLT GRPAYVGDTA LSVAYRHVND
DVPPPSELVP EIPPAVDDLV FRATRRDPAR RPESAEAFLT ELERVRTELG IAPVAVPAPA
SEERTRQLTP PVAAGDPPTE QIPPVRDTPP VGPQRTRAMA RPATGDHTQE FSTVAAPPSG
PERDRRRSRR TVVVWTVLVL VLAALVGGAA YWLGIGSYVQ VPRVVGEQEA AAQQTLEGAD
LTGNVTKEYN NTIAEGVVIS SNPGEGSRVR SGGTVDLVVS LGKPKVPQIA EGTTVAEAES
AIRNVKLQPK HDESGDQYHT TVPEGRVISV NPAPGTALNI STEVTLIVSK GPPPVKVPDV
RGMSRDDAFT TLRNAGFDPY EAGRQFDSGV DGDHVISTDP AIGSELRLVG QPRIGVVLSN
AVQVPSLNGV QVDEAKQQVA ALGLQLSVQE FFERPNMVIL GQYPLPGSRV EPGTTIHATA
F
//
