ARGR_MYCTU
ID ARGR_MYCTU Reviewed; 170 AA.
AC P9WPY9; L0T7J6; P0A4Y8; P94992;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Arginine repressor;
GN Name=argR; Synonyms=ahrC; OrderedLocusNames=Rv1657; ORFNames=MTCY06H11.22;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Regulates arginine biosynthesis genes. {ECO:0000250}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44422.1; -; Genomic_DNA.
DR PIR; D70621; D70621.
DR RefSeq; NP_216173.1; NC_000962.3.
DR RefSeq; WP_003408178.1; NZ_NVQJ01000069.1.
DR PDB; 2ZFZ; X-ray; 1.85 A; A/B/C/D/E/F=92-170.
DR PDB; 3BUE; X-ray; 2.15 A; A/B/C/D/E/F=92-170.
DR PDB; 3CAG; X-ray; 1.90 A; A/B/C/D/E/F=92-170.
DR PDB; 3ERE; X-ray; 2.50 A; D=1-170.
DR PDB; 3FHZ; X-ray; 3.27 A; A/B/C/D/E/F=1-170.
DR PDB; 3LAJ; X-ray; 2.31 A; A/B/C/D/E/F=1-170.
DR PDB; 3LAP; X-ray; 2.15 A; A/B/C/D/E/F=1-170.
DR PDBsum; 2ZFZ; -.
DR PDBsum; 3BUE; -.
DR PDBsum; 3CAG; -.
DR PDBsum; 3ERE; -.
DR PDBsum; 3FHZ; -.
DR PDBsum; 3LAJ; -.
DR PDBsum; 3LAP; -.
DR AlphaFoldDB; P9WPY9; -.
DR SMR; P9WPY9; -.
DR STRING; 83332.Rv1657; -.
DR PaxDb; P9WPY9; -.
DR DNASU; 885091; -.
DR GeneID; 885091; -.
DR KEGG; mtu:Rv1657; -.
DR TubercuList; Rv1657; -.
DR eggNOG; COG1438; Bacteria.
DR OMA; IMGTICG; -.
DR PhylomeDB; P9WPY9; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001584; 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; IDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..170
FT /note="Arginine repressor"
FT /id="PRO_0000205104"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:3LAP"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:3LAP"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:3LAP"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3LAP"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3LAP"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3LAJ"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:3ERE"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:2ZFZ"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:2ZFZ"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:2ZFZ"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:3ERE"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:2ZFZ"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:2ZFZ"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:2ZFZ"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:2ZFZ"
SQ SEQUENCE 170 AA; 17350 MW; A4149C9771DC53A0 CRC64;
MSRAKAAPVA GPEVAANRAG RQARIVAILS SAQVRSQNEL AALLAAEGIE VTQATLSRDL
EELGAVKLRG ADGGTGIYVV PEDGSPVRGV SGGTDRMARL LGELLVSTDD SGNLAVLRTP
PGAAHYLASA IDRAALPQVV GTIAGDDTIL VVAREPTTGA QLAGMFENLR
