ID H6MW15_GORPV Unreviewed; 835 AA.
AC H6MW15;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=pknG {ECO:0000313|EMBL:AFA71710.1};
GN OrderedLocusNames=GPOL_c06410 {ECO:0000313|EMBL:AFA71710.1};
OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA71710.1, ECO:0000313|Proteomes:UP000009154};
RN [1] {ECO:0000313|EMBL:AFA71710.1, ECO:0000313|Proteomes:UP000009154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA Liebl W., Daniel R., Steinbuchel A.;
RT "Involvement of two latex-clearing proteins during rubber degradation and
RT insights into the subsequent degradation pathway revealed by the genome
RT sequence of Gordonia polyisoprenivorans strain VH2.";
RL Appl. Environ. Microbiol. 78:2874-2887(2012).
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; CP003119; AFA71710.1; -; Genomic_DNA.
DR RefSeq; WP_014358683.1; NC_016906.1.
DR AlphaFoldDB; H6MW15; -.
DR STRING; 1112204.GPOL_c06410; -.
DR KEGG; gpo:GPOL_c06410; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_011707_0_0_11; -.
DR OMA; PHCGSAY; -.
DR Proteomes; UP000009154; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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; IPR031634; PknG_rubred.
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; PF16919; PknG_rubred; 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:AFA71710.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009154};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 193..446
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 90341 MW; 0A9E051B0B163774 CRC64;
MTEHDDRTDA EVGTQRVDPA DLDIGTQRAD LGDLDVGTQR ADPTDLDPGT QRADLAALVD
TGMTSSGGRT TTSPVTGSTD PVVRSGPVIP TEALASVGHT RRLVPKRRPQ VHDRRLGTGL
VELPKVVDIE PADAVLDFPV IPEGKRTCWR CGRPVGRNDG EGAGDLAGTC PHCGARYSFV
PGLAPGTVVA GQYEIAGAIA HGGLGWIYLA IDRNVSDRPV VLKGLLNSSD SEAQQVALAE
RQFLASVNHP GIVKIYNFVE HVTADDERFG YIVMEYIGGQ TLKQITSAGA DSGGTHAVMP
IEQAMAYILE VLPAIGYLHS VGLVYNDVKP ENVMVSSDEV KLIDLGAVSA INGYGHLYGT
PGFQAPEIVQ TGPQVVTDIY SIGRTLAVLT LDMPMEKGRY LDGLPDPETT PVLAENPSYY
LLLQRATATD PAERFSSAEE MTTQMLNVLR ETVAVHTGVP RPSLSTVFTP QRSTFGTDLM
LAPVDGFFDP DLAAFYDPVD IAHALPVPLV NPTDPAAGLL NSAALSDPRQ TLDSINAARA
EGFSSLLGRR SNNAHPSLEI DLAEARAHLE LDDVDTALSV LQNVTAQHGE SWRVDWYMGI
CALMNDEPEL AHERFTEVLQ AMPGEVAPKL AAAGTAEIIG RWLTDEKHPS EEEPEESPDA
RIAEMYDVAD RLYHDLWLTD HSIVTAAFGL ARLAVARGDF DAAIEPLDEV PPTSRHYNTA
RATAVLALVH GRAPELVQKR QLVEAARRLE AMPDSEPRKS RLQLIVLGTA MGWIMEHPDE
SGEPSTLLGV PFTERGLRAG TERSLRTLAR QMRNNRDNRF LLVDLANYVR PDSLF
//