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Database: UniProt
Entry: C0PWA3_SALPC
LinkDB: C0PWA3_SALPC
Original site: C0PWA3_SALPC 
ID   C0PWA3_SALPC            Unreviewed;       406 AA.
AC   C0PWA3;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   SubName: Full=N-acetylglucosamine repressor {ECO:0000313|EMBL:ACN44866.1};
GN   Name=nagC {ECO:0000313|EMBL:ACN44866.1};
GN   OrderedLocusNames=SPC_0691 {ECO:0000313|EMBL:ACN44866.1};
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213 {ECO:0000313|EMBL:ACN44866.1, ECO:0000313|Proteomes:UP000001599};
RN   [1] {ECO:0000313|EMBL:ACN44866.1, ECO:0000313|Proteomes:UP000001599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594 {ECO:0000313|EMBL:ACN44866.1,
RC   ECO:0000313|Proteomes:UP000001599};
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
CC   -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family.
CC       {ECO:0000256|ARBA:ARBA00006479}.
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DR   EMBL; CP000857; ACN44866.1; -; Genomic_DNA.
DR   RefSeq; WP_000187578.1; NC_012125.1.
DR   AlphaFoldDB; C0PWA3; -.
DR   KEGG; sei:SPC_0691; -.
DR   HOGENOM; CLU_036604_13_1_6; -.
DR   OMA; VDFGHTH; -.
DR   Proteomes; UP000001599; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000835; HTH_MarR-typ.
DR   InterPro; IPR000600; ROK.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR18964:SF175; N-ACETYLGLUCOSAMINE REPRESSOR; 1.
DR   PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1.
DR   Pfam; PF01047; MarR; 1.
DR   Pfam; PF00480; ROK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS01125; ROK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          25..63
FT                   /note="HTH marR-type"
FT                   /evidence="ECO:0000259|Pfam:PF01047"
SQ   SEQUENCE   406 AA;  44494 MW;  5F2D18ED6319A73C CRC64;
     MTPGGQAQIG NVDLVKQLNS AAVYRLIDQH GPISRIQIAE QSQLAPASVT KITRQLIERG
     LIKEVDQQAS TGGRRAISIV TETRNFHAIG VRLGRHDTTL TLYDLSSKVV AEEHYPLPER
     TQETLEHALL NTIAVFIDSC QRKIRELIAI SVILPGLVDP ESGVIRYMPH IQVENWGLVE
     ALEKRFHVTC FVGHDIRSLA LAEHYFGASQ DCEDSILVRV HRGTGAGIIS NGRIFIGRNG
     NVGEIGHIQV EPLGERCHCG NFGCLETIAA NAAIEQRVLN LLKQGYQSRV PLDDCTIKTI
     CKAANRGDSL ASEVIEHVGR HLGKTIAIAI NLFNPQKIVI AGEIIEADKV LLPAIESCIN
     TQALKAFRKN LPVVRSTLDH RSAIGAFALV KRAMLNGTLL QRLLES
//
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