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Database: UniProt
Entry: W5XWP6_9CORY
LinkDB: W5XWP6_9CORY
Original site: W5XWP6_9CORY 
ID   W5XWP6_9CORY            Unreviewed;       871 AA.
AC   W5XWP6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Serine/threonine protein kinase PknG {ECO:0000313|EMBL:AHI21104.1};
GN   ORFNames=CCASEI_12770 {ECO:0000313|EMBL:AHI21104.1};
OS   Corynebacterium casei LMG S-19264.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1285583 {ECO:0000313|EMBL:AHI21104.1, ECO:0000313|Proteomes:UP000019226};
RN   [1] {ECO:0000313|EMBL:AHI21104.1, ECO:0000313|Proteomes:UP000019226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG S-19264 {ECO:0000313|EMBL:AHI21104.1,
RC   ECO:0000313|Proteomes:UP000019226};
RA   Ruckert C., Albersmeier A., Kalinowski J.;
RT   "The complete genome sequence of Corynebacterium casei LMG S-19264 (=DSM
RT   44701).";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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; CP004350; AHI21104.1; -; Genomic_DNA.
DR   RefSeq; WP_025388189.1; NZ_CP004350.1.
DR   AlphaFoldDB; W5XWP6; -.
DR   STRING; 1285583.CCASEI_12770; -.
DR   GeneID; 82878649; -.
DR   KEGG; ccg:CCASEI_12770; -.
DR   PATRIC; fig|1285583.3.peg.2552; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_011707_0_0_11; -.
DR   OrthoDB; 137117at2; -.
DR   Proteomes; UP000019226; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:AHI21104.1};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:AHI21104.1}; Transferase {ECO:0000313|EMBL:AHI21104.1}.
FT   DOMAIN          225..492
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..118
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   871 AA;  96799 MW;  6EFA6A75327277E1 CRC64;
     MTHNFSDDEL NYLDPAKGKE QPGTEAVAFD PFADDDEEEV NTTAAAEAAA ADAEEERDDV
     EIEALLKQVG ASEGAAATEA VAYDPFADDE LEDEDEGTSA VAFDPFADDD DDTDGHSEES
     FTDSDNIAAL IKDLGVLRDK REKRRGNASA LIDTSQRSRQ QALDTFRELR LAARTNREVA
     DGMVSLPYVV PTDPEYALMD PTEATKEKKL APPQLKPGDI VASQYEILGV IAHGGMGWIY
     LANDHFVSGR VVVLKGMQAH KSADETAAAE AEREFLADIT HPGIVKIFNF IDDARVPGGF
     IVMEYVGGPS LRKRRNALPE RRLPFTIAIA YILELLPALD YLHSRGVVYN DLKPDNIIVT
     EDQVKLIDLG AVSGIGAFGY IYGTKGFQAP EVPTEGPSVS SDIYTIGRTL AALTLKLPHE
     DGVFLPGIPN PTQEPRLRRH VSFYRLLQRA TNPDPKKRFK DISEMRTQLY GVLREIIAIR
     DGIQHPAQHS LFSPARSTFG TKHLVFRTDQ LIDGIERTVR ITAPEVVSAL PTPLLDRDDV
     GAALLQGYSY TEPQEALETL RQAMQTVEYE ESAEIPFGVV RSMLDLGYTG QAKQWLEKLE
     SRLGEDWRFQ WYSGVTQLLL EDFTASQLHF SNMLEILPGE AAPKLALAAV NELLLQSMGY
     SEQQLLEPAV ARACANITSN LYELDDEYFV DQTIWEHISS DPKRIRFNSL RLYGTVWATN
     PTTVSSAFGL ARLLRAENQV EMAVATLDRV PNASRHQRMA RLTTIVQLIS QDVNESRVRR
     AARRLEEIPT NEPRFLQIKI AVITAGLSFL RDSKLQAAAS PNDLFEYAFT ERGLRYGLAD
     TLRALARQAP FSRHRYALVD LANQVRPVTT F
//
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