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
//