ID   Q4JYC1_CORJK            Unreviewed;       722 AA.
AC   Q4JYC1;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 115.
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:CAI36186.1};
GN   OrderedLocusNames=jk0037 {ECO:0000313|EMBL:CAI36186.1};
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI36186.1, ECO:0000313|Proteomes:UP000000545};
RN   [1] {ECO:0000313|EMBL:CAI36186.1, ECO:0000313|Proteomes:UP000000545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411 {ECO:0000313|EMBL:CAI36186.1,
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; CAI36186.1; -; Genomic_DNA.
DR   RefSeq; WP_011272802.1; NC_007164.1.
DR   AlphaFoldDB; Q4JYC1; -.
DR   STRING; 306537.jk0037; -.
DR   GeneID; 3432409; -.
DR   KEGG; cjk:jk0037; -.
DR   PATRIC; fig|306537.10.peg.48; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_135_2_11; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000000545; Chromosome.
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; cd06577; PASTA_pknB; 4.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 4.
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:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF03793; PASTA; 4.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 4.
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:CAI36186.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000545};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:CAI36186.1};
KW   Transferase {ECO:0000313|EMBL:CAI36186.1}.
FT   DOMAIN          12..290
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          445..511
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          512..580
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          581..645
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   722 AA;  76877 MW;  528CE99AF45E7132 CRC64;
     MDRIGTTLGG RYRLGAKIGT GGMSDVYAAT DELLGRDVAV KMMRPDLARD TTFLERFRRE
     AQNAAKLNHP AIVAVYDTGQ TPDEDGAVPY IVMERVHGET LRDIIQDSGK MSLNDAAAVM
     SQVCSALFFS HEAGIIHRDI KPANVMITNT GAVKVMDFGI ARALSDSSSA MTQTAAVIGT
     AQYLSPEQAR GQSADARSDI YAAGCVFYEL ATGKAPFHGE SPLSVAFQHV QENPEAPSQV
     LGMHLSKREA LSLDSITLTA MAKSPSDRYD DAQEMATDLK RLSEDQLPLV AQAYANDADS
     ANAGSHTSGR AAAGAAGLAA GAAAAGVAGA HANGDDVQTS VIPASHSTNN GAAAGMAATG
     GEGGDGYYGE YDDDYEGDDY YDGAYGDEYD DEYGDGYDDE YYEDEPKRRW WAPIAWVAGI
     AAVIAGGYFA YQAFTGDDEP EKPIEAEQVK IPLVANKDRA EAEKILKDAG FEVTVEETTH
     DKIARGKAIG TDPAANASVA RGTEIKLLVS SSREITDVPD LTGKTTEEAV KLLKDAKLVL
     NNEVKEEASD DVPKGKIITQ TPPQGSQVSA GTKVTITVST GPEDVRVPVV TGQQVEDARE
     NLESAGFKVV VNQVDSVEPK GQVLSASSEG EKLAKGSEIT LEVSLGNQFE MPSLQGMKFG
     DVFRELQAAG WRGTPDQLHR ENKNTADLGR VDEVAQQSIH SGQVIKRDED ITVTVYVFNL
     LP
//