ID   MRGA_BACSU              Reviewed;         153 AA.
AC   P37960;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   09-JAN-2013, entry version 91.
DE   RecName: Full=Metalloregulation DNA-binding stress protein;
GN   Name=mrgA; OrderedLocusNames=BSU32990;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
RX   MEDLINE=93374837; PubMed=8396117;
RA   Chen L., James L.P., Helmann J.D.;
RT   "Metalloregulation in Bacillus subtilis: isolation and
RT   characterization of two genes differentially repressed by metal
RT   ions.";
RL   J. Bacteriol. 175:5428-5437(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98015415; PubMed=9353931; DOI=10.1099/00221287-143-10-3305;
RA   Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT   "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT   degrees) in Bacillus subtilis.";
RL   Microbiology 143:3305-3308(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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   CHARACTERIZATION.
RX   MEDLINE=96296451; PubMed=8709848;
RX   DOI=10.1111/j.1365-2958.1995.mmi_18020295.x;
RA   Chen L., Helmann J.D.;
RT   "Bacillus subtilis MrgA is a Dps(PexB) homologue: evidence for
RT   metalloregulation of an oxidative-stress gene.";
RL   Mol. Microbiol. 18:295-300(1995).
CC   -!- FUNCTION: Forms highly stable, multimeric protein-DNA complexes
CC       which accumulate in stationary-phase cells and protect against
CC       oxidative killing.
CC   -!- INDUCTION: By oxidative stress and by growth in minimal medium
CC       lacking iron (Fe(3+)), or one of the divalent cations manganese,
CC       copper or cobalt.
CC   -!- SIMILARITY: Belongs to the dps family.
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DR   EMBL; L19547; AAA68042.1; -; Genomic_DNA.
DR   EMBL; Z22928; CAA80510.1; -; Genomic_DNA.
DR   EMBL; Z93941; CAB07970.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15288.1; -; Genomic_DNA.
DR   PIR; G69660; G69660.
DR   RefSeq; NP_391178.1; NC_000964.3.
DR   PDB; 2CHP; X-ray; 2.00 A; A/B/C/D=1-153.
DR   PDBsum; 2CHP; -.
DR   ProteinModelPortal; P37960; -.
DR   SMR; P37960; 6-153.
DR   EnsemblBacteria; EBBACT00000001083; EBBACP00000001083; EBBACG00000001081.
DR   GeneID; 938592; -.
DR   GenomeReviews; AL009126_GR; BSU32990.
DR   KEGG; bsu:BSU32990; -.
DR   PATRIC; 18978582; VBIBacSub10457_3454.
DR   GenoList; BSU32990; -.
DR   eggNOG; COG0783; -.
DR   HOGENOM; HOG000273542; -.
DR   KO; K04047; -.
DR   OMA; KLHRFHW; -.
DR   ProtClustDB; CLSK887852; -.
DR   BioCyc; BSUB:BSU32990-MONOMER; -.
DR   EvolutionaryTrace; P37960; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0016722; F:oxidoreductase activity, oxidizing metal ions; IEA:InterPro.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1260.10; Ferritin_rel; 1.
DR   InterPro; IPR002177; DPS_DNA-bd.
DR   InterPro; IPR023188; DPS_DNA-bd_CS.
DR   InterPro; IPR012347; Ferritin-rel.
DR   InterPro; IPR009078; Ferritin/RNR-like.
DR   InterPro; IPR008331; Ferritin_DPS_dom.
DR   Pfam; PF00210; Ferritin; 1.
DR   PIRSF; PIRSF005900; Dps; 1.
DR   PRINTS; PR01346; HELNAPAPROT.
DR   SUPFAM; SSF47240; Ferritin/RR_like; 1.
DR   PROSITE; PS00818; DPS_1; 1.
DR   PROSITE; PS00819; DPS_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; DNA-binding; Reference proteome;
KW   Stress response.
FT   CHAIN         1    153       Metalloregulation DNA-binding stress
FT                                protein.
FT                                /FTId=PRO_0000201660.
FT   HELIX         7     37
FT   HELIX        43     70
FT   HELIX        79     85
FT   HELIX        97    124
FT   HELIX       128    151
SQ   SEQUENCE   153 AA;  17332 MW;  3082CF803401E17D CRC64;
     MKTENAKTNQ TLVENSLNTQ LSNWFLLYSK LHRFHWYVKG PHFFTLHEKF EELYDHAAET
     VDTIAERLLA IGGQPVATVK EYTEHASITD GGNETSASEM VQALVNDYKQ ISSESKFVIG
     LAEENQDNAT ADLFVGLIEE VEKQVWMLSS YLG
//