ARGR_VIBVY
ID ARGR_VIBVY Reviewed; 156 AA.
AC Q7MP98;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Arginine repressor {ECO:0000255|HAMAP-Rule:MF_00173};
GN Name=argR {ECO:0000255|HAMAP-Rule:MF_00173}; OrderedLocusNames=VV0466;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
CC -!- FUNCTION: Regulates arginine biosynthesis genes. {ECO:0000255|HAMAP-
CC Rule:MF_00173}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00173}.
CC -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000255|HAMAP-
CC Rule:MF_00173}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC93230.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000037; BAC93230.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011078752.1; NC_005139.1.
DR PDB; 3V4G; X-ray; 1.60 A; A=1-156.
DR PDBsum; 3V4G; -.
DR AlphaFoldDB; Q7MP98; -.
DR SMR; Q7MP98; -.
DR STRING; 672.VV93_v1c04340; -.
DR EnsemblBacteria; BAC93230; BAC93230; BAC93230.
DR GeneID; 66963798; -.
DR KEGG; vvy:VV0466; -.
DR eggNOG; COG1438; Bacteria.
DR HOGENOM; CLU_097103_2_0_6; -.
DR OMA; MVYCLPP; -.
DR OrthoDB; 1640037at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000002675; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034618; F:arginine binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00173; Arg_repressor; 1.
DR InterPro; IPR001669; Arg_repress.
DR InterPro; IPR020899; Arg_repress_C.
DR InterPro; IPR036251; Arg_repress_C_sf.
DR InterPro; IPR020900; Arg_repress_DNA-bd.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR34471; PTHR34471; 1.
DR Pfam; PF01316; Arg_repressor; 1.
DR Pfam; PF02863; Arg_repressor_C; 1.
DR PRINTS; PR01467; ARGREPRESSOR.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF55252; SSF55252; 1.
DR TIGRFAMs; TIGR01529; argR_whole; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..156
FT /note="Arginine repressor"
FT /id="PRO_0000205142"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:3V4G"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:3V4G"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:3V4G"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3V4G"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3V4G"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3V4G"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:3V4G"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:3V4G"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:3V4G"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3V4G"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3V4G"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:3V4G"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:3V4G"
SQ SEQUENCE 156 AA; 17145 MW; FDD795383AE58DA2 CRC64;
MRPSEKQDNL VRAFKALLKE ERFGSQGEIV EALKQEGFEN INQSKVSRML TKFGAVRTRN
AKMEMVYCLP TELGVPTVSS SLRELVLDVD HNQALVVIHT GPGAAQLIAR MLDSLGKSEG
ILGVVAGDDT IFITPTLTIT TEQLFKSVCE LFEYAG