ARGR_BACSU
ID ARGR_BACSU Reviewed; 149 AA.
AC P17893;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Arginine repressor;
DE AltName: Full=Arginine hydroxamate resistance protein;
GN Name=argR; Synonyms=ahrC; OrderedLocusNames=BSU24250;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2507400; DOI=10.1016/0378-1119(89)90247-3;
RA North A.K., Smith M.C.M., Baumberg S.;
RT "Nucleotide sequence of a Bacillus subtilis arginine regulatory gene and
RT homology of its product to the Escherichia coli arginine repressor.";
RL Gene 80:29-38(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-149.
RX PubMed=2106508; DOI=10.1128/jb.172.3.1306-1311.1990;
RA van Hoy B.E., Hoch J.A.;
RT "Characterization of the spoIVB and recN loci of Bacillus subtilis.";
RL J. Bacteriol. 172:1306-1311(1990).
RN [5]
RP PROTEIN SEQUENCE OF 1-30.
RX PubMed=1312212; DOI=10.1111/j.1365-2958.1992.tb02008.x;
RA Czaplewski L.G., North A.K., Smith M.C.M., Baumberg S., Stockley P.G.;
RT "Purification and initial characterization of AhrC: the regulator of
RT arginine metabolism genes in Bacillus subtilis.";
RL Mol. Microbiol. 6:267-275(1992).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=11856827; DOI=10.1107/s0907444901021692;
RA Dennis C.A., Glykos N.M., Parsons M.R., Phillips S.E.;
RT "The structure of AhrC, the arginine repressor/activator protein from
RT Bacillus subtilis.";
RL Acta Crystallogr. D 58:421-430(2002).
CC -!- FUNCTION: Represses the synthesis of biosynthetic enzymes and activates
CC the arginine catabolism. Controls the transcription of the two operons
CC rocABC and rocDEF.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway.
CC -!- SUBUNIT: Homohexamer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000305}.
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DR EMBL; M27869; AAA22208.1; -; Genomic_DNA.
DR EMBL; D84432; BAA12578.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14356.1; -; Genomic_DNA.
DR EMBL; M30297; AAA22690.1; -; Genomic_DNA.
DR PIR; JS0275; JS0275.
DR RefSeq; NP_390305.1; NC_000964.3.
DR RefSeq; WP_003230265.1; NZ_JNCM01000036.1.
DR PDB; 1F9N; X-ray; 2.70 A; A/B/C/D/E/F=1-149.
DR PDB; 2P5K; X-ray; 1.00 A; A=1-64.
DR PDB; 2P5L; X-ray; 2.85 A; C/D/G/H=1-64.
DR PDB; 2P5M; X-ray; 1.95 A; A/B/C=67-149.
DR PDBsum; 1F9N; -.
DR PDBsum; 2P5K; -.
DR PDBsum; 2P5L; -.
DR PDBsum; 2P5M; -.
DR AlphaFoldDB; P17893; -.
DR SMR; P17893; -.
DR STRING; 224308.BSU24250; -.
DR PaxDb; P17893; -.
DR PRIDE; P17893; -.
DR EnsemblBacteria; CAB14356; CAB14356; BSU_24250.
DR GeneID; 938653; -.
DR KEGG; bsu:BSU24250; -.
DR PATRIC; fig|224308.179.peg.2643; -.
DR eggNOG; COG1438; Bacteria.
DR InParanoid; P17893; -.
DR OMA; IMGTICG; -.
DR PhylomeDB; P17893; -.
DR BioCyc; BSUB:BSU24250-MON; -.
DR UniPathway; UPA00068; -.
DR UniPathway; UPA00254; -.
DR EvolutionaryTrace; P17893; -.
DR Proteomes; UP000001570; 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:0019547; P:arginine catabolic process to ornithine; 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;
KW Arginine metabolism; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..149
FT /note="Arginine repressor"
FT /id="PRO_0000205072"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:2P5K"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:2P5K"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:2P5K"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2P5K"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:2P5K"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:2P5K"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:2P5M"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:2P5M"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:2P5M"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:2P5M"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2P5M"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:2P5M"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:2P5M"
SQ SEQUENCE 149 AA; 16832 MW; 3608F3B023FCC293 CRC64;
MNKGQRHIKI REIITSNEIE TQDELVDMLK QDGYKVTQAT VSRDIKELHL VKVPTNNGSY
KYSLPADQRF NPLSKLKRAL MDAFVKIDSA SHMIVLKTMP GNAQAIGALM DNLDWDEMMG
TICGDDTILI ICRTPEDTEG VKNRLLELL
