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Database: UniProt
Entry: A0A172TL30_9BACL
LinkDB: A0A172TL30_9BACL
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ID   A0A172TL30_9BACL        Unreviewed;       723 AA.
AC   A0A172TL30;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=SY83_15680 {ECO:0000313|EMBL:ANE47483.1};
OS   Paenibacillus swuensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1178515 {ECO:0000313|EMBL:ANE47483.1, ECO:0000313|Proteomes:UP000076927};
RN   [1] {ECO:0000313|EMBL:ANE47483.1, ECO:0000313|Proteomes:UP000076927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY6 {ECO:0000313|EMBL:ANE47483.1,
RC   ECO:0000313|Proteomes:UP000076927};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Paenibacillus swuensis/DY6/whole genome sequencing.";
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};
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DR   EMBL; CP011388; ANE47483.1; -; Genomic_DNA.
DR   RefSeq; WP_068608202.1; NZ_CP011388.1.
DR   AlphaFoldDB; A0A172TL30; -.
DR   STRING; 1178515.SY83_15680; -.
DR   KEGG; pswu:SY83_15680; -.
DR   PATRIC; fig|1178515.4.peg.3152; -.
DR   OrthoDB; 9788659at2; -.
DR   Proteomes; UP000076927; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 3.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 3.
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; IPR017441; Protein_kinase_ATP_BS.
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:SF6; SERINE/THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF03793; PASTA; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ANE47483.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000076927};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ANE47483.1};
KW   Transferase {ECO:0000313|EMBL:ANE47483.1}.
FT   DOMAIN          10..270
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          365..432
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          433..502
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          503..572
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          313..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..723
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   723 AA;  79500 MW;  B09EA2E8DEAEE55F CRC64;
     MIGLELGGRY EIISRIGGGG MALVYKGHDI LLNRKVAVKV LRQQFVHDEE FIRRFRREAQ
     SAASLSHPNV VSIYDVGQED EIHYIVMEYI DGHNLNEIIQ ERAPLQAEES VRVASQICDA
     LEHAHQNHII HRDIKPHNIL IGKNGRVKVT DFGIARAVTS STITQTGSVI GSVHYFSPEH
     AKGVVTGEKS DLYSLGIVLY QMLTARLPFL GESPISVALK HLQEQLEEPR RVNPSIPQSV
     ENVILKAMRK NPEERYQSAT EMLKDLETCL RPERVSEPKI AFATFDDGEQ TRVMTAIKPE
     QLAAYKAANG NTSPGAVAAS SKGSTSGSPP PKKKTWVKPF SWIFGTILLL LLMWFGVQWV
     QSILRVPEVA VPNLTGMTLD EARAELIKSG LGVDEPPLYK IDEEVPKDVV LSYDKQGMLV
     RKGDTIKLTV SKGIPLILLS DYEGQQYKDV KASLIAQGVQ EELISDDQVF SDEEAGTIVG
     QSIPANQEMN PKKDALEFTV SKGRETFKMP NLIGFSEAEA KAIAIQNNLR ISDANVKSEP
     SYSPKGVVFR QWPYEPNQPV AENSEVTIYV SSGYPSDALF YTFNVTVSPA ILGQESTVKI
     VYSDARGDNM EWGTKKLKDV QTYPVELVLS PTKDGVISIY RDGKLADSAT VSYDGAVNGD
     QPTMTIPGAE AEPVQGAETP SEEVKPPAEG TTEPPAAQDN GKGKGKDKNK DKKNNDSNDN
     EDD
//
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