ID C4LKQ2_CORK4 Unreviewed; 846 AA.
AC C4LKQ2;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=Serine/threonine protein kinase PknG {ECO:0000313|EMBL:ACR18407.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:ACR18407.1};
GN OrderedLocusNames=ckrop_1682 {ECO:0000313|EMBL:ACR18407.1};
OS Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS CCUG 35717).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR18407.1, ECO:0000313|Proteomes:UP000001473};
RN [1] {ECO:0000313|EMBL:ACR18407.1, ECO:0000313|Proteomes:UP000001473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC {ECO:0000313|Proteomes:UP000001473};
RX PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT revealed insights into the physiology of a lipophilic corynebacterium that
RT lacks mycolic acids.";
RL J. Biotechnol. 136:22-30(2008).
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; CP001620; ACR18407.1; -; Genomic_DNA.
DR RefSeq; WP_012732294.1; NC_012704.1.
DR AlphaFoldDB; C4LKQ2; -.
DR STRING; 645127.ckrop_1682; -.
DR GeneID; 78091902; -.
DR KEGG; ckp:ckrop_1682; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_011707_0_0_11; -.
DR OMA; PHCGSAY; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000001473; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR031636; PknG_TPR.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE/THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF16918; PknG_TPR; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ACR18407.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001473};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:ACR18407.1}; Transferase {ECO:0000313|EMBL:ACR18407.1}.
FT DOMAIN 197..442
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 846 AA; 92707 MW; 45824F88B15E1530 CRC64;
MSDSEPNVRD EGLGADETRD SEAGLNSDAA QDSEDNARDT DNGRPDDNDH PTEAATVMGT
RAVPFDPFAD DDDDDEIDID INDIGSLLQS DNPADTPSSG DGVTGPGPGS AKTVARPRGA
DGASHDPSQA SRERALSTFR ERRAASRRGK VVADGMVPLP FIVPTDPRES VMDSDTIKET
DAKAPSLHKG DMVAGQYEVV GALANGGVGW IYLAIDHNVS DRWVVLKGMK ATANEQDRAV
AGAERAFLAD ITHTGIVKIY NFVDDDRSPG GFIVMEYVGG PSLRSQRKKQ RDSLFAVDVA
IGYMLEVLEA LDYLHSRGVV YNDLKPDNII ITEEQVKLID LGAVTGIGAF GHIYGTPGFQ
APEITETGPT VRSDIYTVGR TLASLIVHLP TVDGRYEDGL PTPTNEPVFR RYLSLYRLLL
RATDPDPEKR FASASSMANQ LTGVLREIRA VRDQVHFPHL HSQFAPQRTT YGTKHLVFRT
DQLVDGIERS IEITAPEVVA ALPVPMVDAT DPGAYILSTI SYAEPSEAID SLYAKMKMPE
YAESVEIPLS IVRAMLDLGL VDEAHNYLST FESSFTRDWR YEWYSGITAL LLNDYEQAQR
HFEKVIFILP GEPAAKLAIA ATSELWLQAK GLSMTSVLDR QTAVAAATLG HASALPSDSA
LEAMGDRWDP VGDDPVALRF HATRLYGLVW ATNPTTVSSA FGLSRQFIAE GDVARAVEAL
DQVPQASRHH RLARLTTVLH LISGPPKDLT EERIIDAAQR LDEIPTNEPR MAQVRVAVMS
AGLNWLRETN RTHATVPTLF GQPFEVRGLR LGVEADLRRM ARSVQYPSHR YHLVDMANAI
RPRTWW
//