MRGA_BACSU
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 03-AUG-2022, entry version 131.
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 PubMed=8396117; DOI=10.1128/jb.175.17.5428-5437.1993;
RA Chen L., James L.P., Helmann J.D.;
RT "Metalloregulation in Bacillus subtilis: isolation and characterization of
RT two genes differentially repressed by metal ions.";
RL J. Bacteriol. 175:5428-5437(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX 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 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 CHARACTERIZATION.
RX PubMed=8709848; 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 which
CC accumulate in stationary-phase cells and protect against oxidative
CC killing.
CC -!- INDUCTION: By oxidative stress and by growth in minimal medium lacking
CC iron (Fe(3+)), or one of the divalent cations manganese, copper or
CC cobalt.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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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 RefSeq; WP_003228537.1; NZ_JNCM01000033.1.
DR PDB; 2CHP; X-ray; 2.00 A; A/B/C/D=1-153.
DR PDBsum; 2CHP; -.
DR AlphaFoldDB; P37960; -.
DR SMR; P37960; -.
DR STRING; 224308.BSU32990; -.
DR jPOST; P37960; -.
DR PaxDb; P37960; -.
DR PRIDE; P37960; -.
DR EnsemblBacteria; CAB15288; CAB15288; BSU_32990.
DR GeneID; 938592; -.
DR KEGG; bsu:BSU32990; -.
DR PATRIC; fig|224308.179.peg.3575; -.
DR eggNOG; COG0783; Bacteria.
DR InParanoid; P37960; -.
DR OMA; NTQLSNW; -.
DR PhylomeDB; P37960; -.
DR BioCyc; BSUB:BSU32990-MON; -.
DR EvolutionaryTrace; P37960; -.
DR Proteomes; UP000001570; Chromosome.
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, acting on metal ions; IEA:InterPro.
DR CDD; cd01043; DPS; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR002177; DPS_DNA-bd.
DR InterPro; IPR023188; DPS_DNA-bd_CS.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR PANTHER; PTHR42932; PTHR42932; 1.
DR Pfam; PF00210; Ferritin; 1.
DR PIRSF; PIRSF005900; Dps; 1.
DR PRINTS; PR01346; HELNAPAPROT.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00818; DPS_1; 1.
DR PROSITE; PS00819; DPS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Stress response.
FT CHAIN 1..153
FT /note="Metalloregulation DNA-binding stress protein"
FT /id="PRO_0000201660"
FT HELIX 7..37
FT /evidence="ECO:0007829|PDB:2CHP"
FT HELIX 43..70
FT /evidence="ECO:0007829|PDB:2CHP"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:2CHP"
FT HELIX 97..124
FT /evidence="ECO:0007829|PDB:2CHP"
FT HELIX 128..151
FT /evidence="ECO:0007829|PDB:2CHP"
SQ SEQUENCE 153 AA; 17332 MW; 3082CF803401E17D CRC64;
MKTENAKTNQ TLVENSLNTQ LSNWFLLYSK LHRFHWYVKG PHFFTLHEKF EELYDHAAET
VDTIAERLLA IGGQPVATVK EYTEHASITD GGNETSASEM VQALVNDYKQ ISSESKFVIG
LAEENQDNAT ADLFVGLIEE VEKQVWMLSS YLG
