ID A0A329KBH5_9BACL Unreviewed; 688 AA.
AC A0A329KBH5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=pknB {ECO:0000313|EMBL:RAU92937.1};
GN ORFNames=DQG13_26585 {ECO:0000313|EMBL:RAU92937.1};
OS Paenibacillus sp. YN15.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1742774 {ECO:0000313|EMBL:RAU92937.1, ECO:0000313|Proteomes:UP000251619};
RN [1] {ECO:0000313|EMBL:RAU92937.1, ECO:0000313|Proteomes:UP000251619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YN15 {ECO:0000313|EMBL:RAU92937.1,
RC ECO:0000313|Proteomes:UP000251619};
RA Niu L.;
RT "Paenibacillus sp.YN15.";
RL Submitted (JUN-2018) 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:RAU92937.1}.
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DR EMBL; QMFA01000049; RAU92937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329KBH5; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000251619; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 2.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 2.
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:SF37; SERINE_THREONINE-PROTEIN KINASE A; 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:RAU92937.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000251619};
KW Transferase {ECO:0000313|EMBL:RAU92937.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 322..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..270
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 353..417
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 418..487
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 488..560
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 646..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..676
FT /note="Polar 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 688 AA; 75643 MW; 5208FF1F71856EDF CRC64;
MIGETLGGRY EILERVGGGG MALVYKAQDL LLNRYVAVKV LRQQYVHDEE FIRRFRREAQ
SAASLSHPNV VSMYDVGQEG DNHFIVMEYV EGMTLNDLIR EKAPLQVEDA LHIATQICDA
LEHAHHNQII HRDIKPHNIL IGKNGRIKVT DFGIARATTS STITQTGSVV GSVHYFSPEH
AKGISTGAKS DLYSLGIVLY QMLTGKLPFL GESPISVALK HLQENVEEPR KVNPLIPQSV
ENIILKAMRK NPDERYQSAS DMLQDLETAL DPKRRNEPKL TFLDDGLDVE ATRVLPALRP
GAGLEVEVRD GSEAEFRKKR NIWIAPLVWT GIFLVFLSVM WFWVIPGFKD KIIPKDVVVP
QVVGKMQSEA ESLLTQAGFQ VVAEPQFSDK PVGQVFKRTP DGAKLKENTE ITLLVSKGAE
KQMMQSYKNR LFKDVKAELL AAGLQEDQIL SDAVFSELPE DTIVNQEPAV GAEFDPVNGK
VKFYYSKGRQ TVIMPDLVNS TVAEAEAKLL SVGLKLAAGE NGRENVESFD VPSGRVVDTH
PYKTGDPVEP SMEIKLFVSS GPPKDAVTYT ASKKLTAATS GKSSIFRIVI SDAKFDNEDY
NTMEVSGSEI INVKVTLTKE KSATILIYRD NVLWDSETIN YQNYLDQKTK PSASPTPTAP
SASPSAAASP TATHAAGSVK PSPKPSGG
//
