ID A0A2N5N7L8_9BACL Unreviewed; 723 AA.
AC A0A2N5N7L8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Serine/threonine protein kinase PrkC, regulator of stationary phase {ECO:0000313|EMBL:PLT46328.1};
GN ORFNames=B8V81_4759 {ECO:0000313|EMBL:PLT46328.1};
OS Paenibacillus pasadenensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=217090 {ECO:0000313|EMBL:PLT46328.1, ECO:0000313|Proteomes:UP000234789};
RN [1] {ECO:0000313|EMBL:PLT46328.1, ECO:0000313|Proteomes:UP000234789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R16 {ECO:0000313|EMBL:PLT46328.1,
RC ECO:0000313|Proteomes:UP000234789};
RA Passera A., Marcolungo L., Casati P., Brasca M., Quaglino F.,
RA Delledonne M.;
RT "Functional genome analysis of Paenibacillus pasadenensis strain R16:
RT insights on endophytic life style and antifungal activity.";
RL Submitted (MAY-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 -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:PLT46328.1}.
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DR EMBL; NFEZ01000004; PLT46328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5N7L8; -.
DR Proteomes; UP000234789; Unassembled WGS sequence.
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; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:PLT46328.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:PLT46328.1};
KW Transferase {ECO:0000313|EMBL:PLT46328.1}.
FT DOMAIN 10..270
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 371..438
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 439..509
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 510..579
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 306..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..689
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..711
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 723 AA; 77897 MW; F2E4C872D968F427 CRC64;
MIGRELGGRY EILTRIGGGG MALVYKAHDL LLSRNVAVKV LRQQYVHDEE FIRRFRREAQ
SAAALSHPNV VSIYDVGQEE EIHYIVMECV DGQNLNEVIQ ERAPLQADEA VRIAAQIADA
LDHAHQNHII HRDIKPHNIL IGKNGRVKVT DFGIARAVTS STITQTGSVI GSVHYFSPEH
AKGVSAGEKS DIYSLGIVLY QMVTGKLPFL GESPISVALK HLQEPLEDPR TVNPLVPQSV
ENIIIKALRK NPSERYRSAG EMLEDLETAL SPARRNEPKL QFGGGDFDET RVMPAIRPGL
GLKESVRAGA EPPPLPEDGH ATARQEAVDE EQDEEPARRR GWVKPLVIVL STLAVLAAVY
GVFRLVSGSL DVAEVDVPYV VGMTETDAKA ALEAKGLLLE EPSIRAFKPD VPKDQVFAQS
KSNMRVKTGS RVRLSISDGP ELKQLGDYKG QKASDVVAAL RALGVPEGSI RLNEVADDSA
EPGVVLSQEP GANSQLDPLV DTVTLTVSKG PETVKMPDLV GKTTEEARKL IADAGLQLRE
DNIVKEGSYR PEGEVLSQFP YDAGSPARKG EQVSITVSSG LPKDALEYTF DLLISPARAG
KASEIRIVYT DATGKDIEAH KRAIKDTRSF PVKVVLAPNT EAFVSVYRDG QLADTFSRTY
DEVKSGADSG PTTVPGSEPS PPPVASPETS PSADPNAAAS PDGQSDGQET AFGSGDGEDG
HDD
//
