ID   Q4JTE8_CORJK            Unreviewed;       470 AA.
AC   Q4JTE8;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 108.
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=pknJ {ECO:0000313|EMBL:CAI37909.1};
GN   OrderedLocusNames=jk1732 {ECO:0000313|EMBL:CAI37909.1};
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI37909.1, ECO:0000313|Proteomes:UP000000545};
RN   [1] {ECO:0000313|EMBL:CAI37909.1, ECO:0000313|Proteomes:UP000000545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411 {ECO:0000313|EMBL:CAI37909.1,
RC   ECO:0000313|Proteomes:UP000000545};
RX   PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI37909.1; -; Genomic_DNA.
DR   RefSeq; WP_011274100.1; NC_007164.1.
DR   AlphaFoldDB; Q4JTE8; -.
DR   STRING; 306537.jk1732; -.
DR   GeneID; 3432411; -.
DR   KEGG; cjk:jk1732; -.
DR   PATRIC; fig|306537.10.peg.1754; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_040779_0_0_11; -.
DR   Proteomes; UP000000545; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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:CAI37909.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000545};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:CAI37909.1};
KW   Transferase {ECO:0000313|EMBL:CAI37909.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        321..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..300
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   470 AA;  50870 MW;  B491C8A1810FB40E CRC64;
     MNLSHPPAPE DFLNDLSVLG YSNVQQLGQG GMGTVFRAYK QNLDRTVAIK VVSQDRVSDT
     EYVNRFHAEM RTMAALDHPA IVPVYDGGVT AHGFPYFAMK YIEGENLHEF LRRRRAIRQP
     LTVQEVAQIL APIASALDYL AALPNPVVHR DIKPANILLP SSDVSDPPAL LTDFGIAIDR
     ESTRMTRVGM RIGTDGYTAP ELLATKDVTE PPQPNALSEQ YSLGLVAFEL LTGIYVRGSV
     TDEQWAVNRP VPELKSHLIH PADVSSIKAV NGVFARVLAV NPHKRFATAS EFISALQSAV
     AAHQSANLVR DVGRSALSKK LLTLVATVVV IATIVSAGVW HFSASQWEGE DARLASKFPE
     IVSEKSGGAG WQSTSCEHRE PGTGELARIA CNSDRLSVVI AHFDSVEARD AVVPAEGAQT
     MKSSRCSALT MPMESSDSAF GVFPQGDLST YGIIVSGENA EDLRLKLPMC
//