ARGR_ALKMQ
ID ARGR_ALKMQ Reviewed; 149 AA.
AC A6TR45;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Arginine repressor {ECO:0000255|HAMAP-Rule:MF_00173};
GN Name=argR {ECO:0000255|HAMAP-Rule:MF_00173}; OrderedLocusNames=Amet_2510;
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF;
RX PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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; CP000724; ABR48663.1; -; Genomic_DNA.
DR RefSeq; WP_012063638.1; NC_009633.1.
DR AlphaFoldDB; A6TR45; -.
DR SMR; A6TR45; -.
DR STRING; 293826.Amet_2510; -.
DR EnsemblBacteria; ABR48663; ABR48663; Amet_2510.
DR KEGG; amt:Amet_2510; -.
DR eggNOG; COG1438; Bacteria.
DR HOGENOM; CLU_097103_3_0_9; -.
DR OMA; VVIHTEL; -.
DR OrthoDB; 1640037at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001572; 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; 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..149
FT /note="Arginine repressor"
FT /id="PRO_1000058318"
SQ SEQUENCE 149 AA; 16829 MW; 510A6506CB641197 CRC64;
MKYSRHAKIL EIIDTMEIET QEELSEELRK IGFNVTQATV SRDIKELRLI KVLSKSGNYK
YATLRSQENV LSDRLVRLFK DSILSIEYAG NIMVMKTLAG AAQAAASAID AVDLKGVMGT
IAGDDTIFVV VRDQDQMQEI EEKFRRLTK