ID A0A0F5VUF4_9ACTN Unreviewed; 639 AA.
AC A0A0F5VUF4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=TN53_26920 {ECO:0000313|EMBL:KKD04995.1};
OS Streptomyces sp. WM6386.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415558 {ECO:0000313|EMBL:KKD04995.1, ECO:0000313|Proteomes:UP000033641};
RN [1] {ECO:0000313|EMBL:KKD04995.1, ECO:0000313|Proteomes:UP000033641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6386 {ECO:0000313|EMBL:KKD04995.1,
RC ECO:0000313|Proteomes:UP000033641};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (JAN-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:KKD04995.1}.
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DR EMBL; JXTE01000049; KKD04995.1; -; Genomic_DNA.
DR RefSeq; WP_046261257.1; NZ_JXTE01000049.1.
DR AlphaFoldDB; A0A0F5VUF4; -.
DR PATRIC; fig|1415558.3.peg.5900; -.
DR Proteomes; UP000033641; 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-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; 2.
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:KKD04995.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000033641};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:KKD04995.1};
KW Transferase {ECO:0000313|EMBL:KKD04995.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 351..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..275
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 372..439
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 440..506
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 507..574
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 575..639
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 327..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 67707 MW; C71E2D4F2CC39ADD CRC64;
MDTTLQDPLV GQVLDGRYRV DARIAVGGMA TVYRAVDTRL DRVLALKVMH PGLAADVTFV
DRFIREAKSV ARLAHPNVVQ VFDQGTDGSY VYLAMEYVAG CTLRDVLRDR GALQPRAALD
ILEPVLAALG AAHRAGFVHR DMKPENVLIG DDGRVKVADF GLVRSVDTVT NTTGTVLGTV
SYLAPEQIES GTADPRVDVY ACGVVFYEML TGEKPHDGDS PAVVLYKHLH EDVPAPSGIV
PGLAFELDEL VASATARTPD IRPYDAVALL AQARAARGAL SEDQLDLVPP QALSVAHSGA
EDRTSVIPRS LTVPRPLPVN EDGAALHHTS RFESPPPPPP RRRSGPPRGP LAIVVALLLI
LGVGAGVWYI NSGQFTKVPA LIDKTEVQAR DRLEEAGLEV GKVKQEYSDT VKRGRVIGSD
PSVGTRIRSN DSVTLTVSKG PETVKLGDLK GLRLDKARAR LKGDGLEPGM VTREFSDDVI
KGFVISTDPE AGTTLRSGAA VALVVSKGSP VDVPDVTGES LEDAKADLTD AGLKVKVSAQ
QVNSEYDKGM VAAQTPQDGS EAAEGDTVTL TISKGPEMVE VPDVVGDSVD DAKAELEGAG
FEVDEDRGIL GLFGDTVKNQ SVEGGETAPK GSTITIEIR
//
