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Database: UniProt
Entry: C4LKQ2_CORK4
LinkDB: C4LKQ2_CORK4
Original site: C4LKQ2_CORK4 
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
//
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