ID A0A927CZ58_9BACI Unreviewed; 150 AA.
AC A0A927CZ58;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 02-APR-2025, entry version 8.
DE RecName: Full=Arginine repressor {ECO:0000256|HAMAP-Rule:MF_00173, ECO:0000256|NCBIfam:TIGR01529};
GN Name=argR {ECO:0000256|HAMAP-Rule:MF_00173,
GN ECO:0000313|EMBL:MBD3108014.1};
GN ORFNames=IEO70_06510 {ECO:0000313|EMBL:MBD3108014.1};
OS Peribacillus faecalis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Peribacillus.
OX NCBI_TaxID=2772559 {ECO:0000313|EMBL:MBD3108014.1, ECO:0000313|Proteomes:UP000602076};
RN [1] {ECO:0000313|EMBL:MBD3108014.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AGMB 02131 {ECO:0000313|EMBL:MBD3108014.1};
RA Jiang L., Lee J.;
RT "Bacillus faecalis sp. nov., a moderately halophilic bacterium isolated
RT from cow faeces.";
RL Submitted (SEP-2020) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MBD3108014.1}.
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DR EMBL; JACXSI010000012; MBD3108014.1; -; Genomic_DNA.
DR RefSeq; WP_190997604.1; NZ_JACXSI010000012.1.
DR Proteomes; UP000602076; 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:L-arginine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR GO; GO:1900079; P:regulation of arginine biosynthetic process; IEA:UniProtKB-UniRule.
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:UP000602076};
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..66
FT /note="Arginine repressor DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF01316"
FT DOMAIN 82..146
FT /note="Arginine repressor C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02863"
SQ SEQUENCE 150 AA; 17384 MW; 719DCC0BDB1EF1FD CRC64;
MNKDRRHFFL RKIIEEHEVE KQEQLVELLN ANGMEVTQAT ISRDIKELNL AKVPTKNGTL
KYAFITNKNV DAQYQKLLRK IQEVVEKIDC VDHLLVIRTI PGNAHVIGAL LDEMQWEEMM
GCVCGNDTCL IITRTEQDTE TLYNRLIKKS
//
