ID A0A1H9LWF5_9BACI Unreviewed; 149 AA.
AC A0A1H9LWF5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Arginine repressor {ECO:0000256|HAMAP-Rule:MF_00173};
GN Name=argR {ECO:0000256|HAMAP-Rule:MF_00173};
GN ORFNames=SAMN04487944_101435 {ECO:0000313|EMBL:SER15776.1};
OS Gracilibacillus ureilyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=531814 {ECO:0000313|EMBL:SER15776.1, ECO:0000313|Proteomes:UP000199687};
RN [1] {ECO:0000313|EMBL:SER15776.1, ECO:0000313|Proteomes:UP000199687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7727 {ECO:0000313|EMBL:SER15776.1,
RC ECO:0000313|Proteomes:UP000199687};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates arginine biosynthesis genes. {ECO:0000256|HAMAP-
CC 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; FOGL01000001; SER15776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9LWF5; -.
DR STRING; 531814.SAMN04487944_101435; -.
DR OrthoDB; 9807089at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000199687; Unassembled WGS sequence.
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:UP000199687};
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 1..70
FT /note="Arginine repressor DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF01316"
FT DOMAIN 81..145
FT /note="Arginine repressor C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02863"
SQ SEQUENCE 149 AA; 16995 MW; 78F91CF2FCC6D462 CRC64;
MNKAQRHIKI REIITENEVE TQDDLVVHFK DLGYTITQAT ISRDIKELHL VKVPTSEGKY
KYSLPADQKF NPLNKLRRFI MDAFVSIDTA THFIVMKTLP GNAQAMGALI DNLSWEEIIG
TICGDDTILI ICKTVDDAEK IKNQFLEML
//