PKN2_CORGL
ID PKN2_CORGL Reviewed; 469 AA.
AC Q8NU97; Q8RQP0;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Serine/threonine-protein kinases PknA;
DE EC=2.7.11.1;
GN Name=pknA; Synonyms=drp72; OrderedLocusNames=Cgl0042, cg0059;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hirano S., Kimura E., Kawahara Y., Sugimoto S.;
RT "drp72 of Corynebacterium glutamicum.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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 -!- 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;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB88662.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB083046; BAB88662.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BA000036; BAB97435.1; -; Genomic_DNA.
DR EMBL; BX927148; CAF18610.1; -; Genomic_DNA.
DR RefSeq; NP_599294.1; NC_003450.3.
DR RefSeq; WP_011013341.1; NC_006958.1.
DR AlphaFoldDB; Q8NU97; -.
DR SMR; Q8NU97; -.
DR DIP; DIP-48320N; -.
DR IntAct; Q8NU97; 1.
DR STRING; 196627.cg0059; -.
DR PRIDE; Q8NU97; -.
DR KEGG; cgb:cg0059; -.
DR KEGG; cgl:Cgl0042; -.
DR PATRIC; fig|196627.13.peg.43; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_000288_63_44_11; -.
DR OMA; YLCEHSV; -.
DR BRENDA; 2.7.11.1; 960.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:CACAO.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IDA:CACAO.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..469
FT /note="Serine/threonine-protein kinases PknA"
FT /id="PRO_0000171199"
FT DOMAIN 20..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 286..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 119
FT /note="R -> S (in Ref. 1; BAB88662)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="D -> N (in Ref. 1; BAB88662)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 50375 MW; 53C10AD97BB95595 CRC64;
MSQEDITGKD RLQELIGADY RLQWIIGHGG MSTVWLADDV VNDREVAIKV LRPEFSDNQE
FLNRFRNEAQ AAENIDSEHV VATYDYREVP DPAGHTFCFI VMEFVRGESL ADLLEREGRL
PEDLALDVME QAAHGLSVIH RMDMVHRDIK PGNMLITANG IVKITDFGIA KAAAAVPLTR
TGMVVGTAQY VSPEQAQGKE VTAASDIYSL GVVGYEMMAG RRPFTGDSSV SVAIAHINQA
PPQMPTSISA QTRELIGIAL RKDPGRRFPD GNEMALAVSA VRLGKRPPQP RTSAMMAQAE
APSPSESTAM LGRVARPATI TQEAAPKRGS GIGIGLFIAA LLAVIIGAVI YAGTTGILFN
DTPEETTTPE TITETYTPTV EETTSQWVPP TPPTRSTFTE PETTSHRPTT SEESTSEEPT
TEAPTSSRTV PQIPTSTPRT SASVPVETNA PADDLIDAVN GLLDVGGAQ
