(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 152.
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}.
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   SMR; P17893; -.
DR   STRING; 224308.BSU24250; -.
DR   PaxDb; P17893; -.
DR   PRIDE; P17893; -.
DR   EnsemblBacteria; CAB14356; CAB14356; BSU24250.
DR   GeneID; 938653; -.
DR   KEGG; bsu:BSU24250; -.
DR   PATRIC; fig|224308.179.peg.2643; -.
DR   eggNOG; ENOG4105XBY; Bacteria.
DR   eggNOG; COG1438; LUCA.
DR   HOGENOM; HOG000242732; -.
DR   InParanoid; P17893; -.
DR   KO; K03402; -.
DR   OMA; IMGTICG; -.
DR   PhylomeDB; P17893; -.
DR   BioCyc; BSUB:BSU24250-MONOMER; -.
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;
DR   PRODOM; P17893.
DR   SWISS-2DPAGE; P17893.
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:0000244|PDB:2P5K"
FT   HELIX           22..31
FT                   /evidence="ECO:0000244|PDB:2P5K"
FT   HELIX           38..48
FT                   /evidence="ECO:0000244|PDB:2P5K"
FT   STRAND          51..55
FT                   /evidence="ECO:0000244|PDB:2P5K"
FT   TURN            56..58
FT                   /evidence="ECO:0000244|PDB:2P5K"
FT   STRAND          59..63
FT                   /evidence="ECO:0000244|PDB:2P5K"
FT   HELIX           72..83
FT                   /evidence="ECO:0000244|PDB:2P5M"
FT   STRAND          84..90
FT                   /evidence="ECO:0000244|PDB:2P5M"
FT   STRAND          93..99
FT                   /evidence="ECO:0000244|PDB:2P5M"
FT   HELIX           103..111
FT                   /evidence="ECO:0000244|PDB:2P5M"
FT   STRAND          120..123
FT                   /evidence="ECO:0000244|PDB:2P5M"
FT   STRAND          125..131
FT                   /evidence="ECO:0000244|PDB:2P5M"
FT   HELIX           135..146
FT                   /evidence="ECO:0000244|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
//

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