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Database: UniProt
Entry: H6MW15_GORPV
LinkDB: H6MW15_GORPV
Original site: H6MW15_GORPV 
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
//
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