ARGR_ALIF1
ID ARGR_ALIF1 Reviewed; 156 AA.
AC Q5E876;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Arginine repressor {ECO:0000255|HAMAP-Rule:MF_00173};
GN Name=argR {ECO:0000255|HAMAP-Rule:MF_00173}; OrderedLocusNames=VF_0275;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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}.
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DR EMBL; CP000020; AAW84770.1; -; Genomic_DNA.
DR RefSeq; WP_011261093.1; NC_006840.2.
DR RefSeq; YP_203658.1; NC_006840.2.
DR AlphaFoldDB; Q5E876; -.
DR SMR; Q5E876; -.
DR STRING; 312309.VF_0275; -.
DR EnsemblBacteria; AAW84770; AAW84770; VF_0275.
DR KEGG; vfi:VF_0275; -.
DR PATRIC; fig|312309.11.peg.270; -.
DR eggNOG; COG1438; Bacteria.
DR HOGENOM; CLU_097103_2_0_6; -.
DR OMA; MVYCLPP; -.
DR OrthoDB; 1640037at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000000537; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; DNA-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..156
FT /note="Arginine repressor"
FT /id="PRO_1000023612"
SQ SEQUENCE 156 AA; 17196 MW; E9BE2737D02AA355 CRC64;
MRNNEKQELL VKEFKAILKA ERFGSQGEIV DALRQSGFDN INQSKVSRML TKFGAVRTRN
AKMEMVYCLP VELGVPTVSS SLRELVMDID YNNALVVIHT GPGAAQLIAR LLDSLGKAEG
ILGVVAGDDT IFITPTRNIE VAELFDSVCD LFEYSV