ID H6N4P7_GORPV Unreviewed; 170 AA.
AC H6N4P7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Arginine repressor {ECO:0000256|ARBA:ARBA00021148, ECO:0000256|HAMAP-Rule:MF_00173};
GN Name=argR {ECO:0000256|HAMAP-Rule:MF_00173,
GN ECO:0000313|EMBL:AFA73629.1};
GN OrderedLocusNames=GPOL_c26070 {ECO:0000313|EMBL:AFA73629.1};
OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA73629.1, ECO:0000313|Proteomes:UP000009154};
RN [1] {ECO:0000313|EMBL:AFA73629.1, 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 -!- FUNCTION: Regulates arginine biosynthesis genes.
CC {ECO:0000256|ARBA:ARBA00002095, ECO:0000256|HAMAP-Rule:MF_00173}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
CC {ECO:0000256|HAMAP-Rule:MF_00173}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00173}.
CC -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000256|ARBA:ARBA00008316,
CC ECO:0000256|HAMAP-Rule:MF_00173}.
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DR EMBL; CP003119; AFA73629.1; -; Genomic_DNA.
DR RefSeq; WP_014360211.1; NC_016906.1.
DR AlphaFoldDB; H6N4P7; -.
DR STRING; 1112204.GPOL_c26070; -.
DR KEGG; gpo:GPOL_c26070; -.
DR eggNOG; COG1438; Bacteria.
DR HOGENOM; CLU_097103_1_1_11; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000009154; Chromosome.
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; 3.30.1360.40; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 NCBIfam; TIGR01529; argR_whole; 1.
DR PANTHER; PTHR34471; ARGININE REPRESSOR; 1.
DR PANTHER; PTHR34471:SF1; ARGININE REPRESSOR; 1.
DR Pfam; PF01316; Arg_repressor; 1.
DR Pfam; PF02863; Arg_repressor_C; 1.
DR PRINTS; PR01467; ARGREPRESSOR.
DR SUPFAM; SSF55252; C-terminal domain of arginine repressor; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00173};
KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00173};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00173};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00173}; Reference proteome {ECO:0000313|Proteomes:UP000009154};
KW Repressor {ECO:0000256|HAMAP-Rule:MF_00173};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00173};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_00173}.
FT DOMAIN 17..85
FT /note="Arginine repressor DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF01316"
FT DOMAIN 101..167
FT /note="Arginine repressor C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02863"
SQ SEQUENCE 170 AA; 17782 MW; DC3415EEC4E5D4A4 CRC64;
MTASSRPEQP ETRLASTRAG RHALIVDILA KNQVRSQSEL QNLLSARGID ATQATISRDL
DELGAVKLRA ADGGVGVYVV PEDGSPVRGV FGGTDRLSRL LSELLVSTDA SGNLAVLRTP
PGAAHYLASA IDRASLPDVV GTIAGDDTIF VCARDPIDGA ELARRIEGLV
//
