ID   MRAZ_YERP3              Reviewed;         152 AA.
AC   A7FM75;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Transcriptional regulator MraZ;
GN   Name=mraZ {ECO:0000255|HAMAP-Rule:MF_01008};
GN   OrderedLocusNames=YpsIP31758_3396;
OS   Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP 31758;
RX   PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA   Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA   Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT   "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT   causative agent of Far East scarlet-like fever.";
RL   PLoS Genet. 3:1508-1523(2007).
CC   -!- FUNCTION: Negatively regulates its own expression and that of the
CC       subsequent genes in the proximal part of the division and cell wall
CC       (dcw) gene cluster. Acts by binding directly to DNA. May also regulate
CC       the expression of genes outside the dcw cluster. {ECO:0000255|HAMAP-
CC       Rule:MF_01008}.
CC   -!- SUBUNIT: Forms oligomers. {ECO:0000255|HAMAP-Rule:MF_01008}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP-
CC       Rule:MF_01008}.
CC   -!- SIMILARITY: Belongs to the MraZ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01008}.
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DR   EMBL; CP000720; ABS45970.1; -; Genomic_DNA.
DR   RefSeq; WP_011191730.1; NC_009708.1.
DR   AlphaFoldDB; A7FM75; -.
DR   SMR; A7FM75; -.
DR   EnsemblBacteria; ABS45970; ABS45970; YpsIP31758_3396.
DR   GeneID; 66842900; -.
DR   KEGG; ypi:YpsIP31758_3396; -.
DR   HOGENOM; CLU_107907_2_0_6; -.
DR   OMA; RGQERCL; -.
DR   Proteomes; UP000002412; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd16321; MraZ_C; 1.
DR   CDD; cd16320; MraZ_N; 1.
DR   Gene3D; 3.40.1550.20; -; 1.
DR   HAMAP; MF_01008; MraZ; 1.
DR   InterPro; IPR003444; MraZ.
DR   InterPro; IPR035644; MraZ_C.
DR   InterPro; IPR020603; MraZ_dom.
DR   InterPro; IPR035642; MraZ_N.
DR   InterPro; IPR038619; MraZ_sf.
DR   InterPro; IPR007159; SpoVT-AbrB_dom.
DR   InterPro; IPR037914; SpoVT-AbrB_sf.
DR   PANTHER; PTHR34701; PTHR34701; 1.
DR   Pfam; PF02381; MraZ; 2.
DR   SUPFAM; SSF89447; SSF89447; 1.
DR   TIGRFAMs; TIGR00242; TIGR00242; 1.
DR   PROSITE; PS51740; SPOVT_ABRB; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; Repeat; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..152
FT                   /note="Transcriptional regulator MraZ"
FT                   /id="PRO_1000062949"
FT   DOMAIN          5..52
FT                   /note="SpoVT-AbrB 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01076"
FT   DOMAIN          81..124
FT                   /note="SpoVT-AbrB 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01076"
SQ   SEQUENCE   152 AA;  17472 MW;  5CBAF40C2DC342F2 CRC64;
     MFRGATMVNL DSKGRLAVPT RYRESLNEES QGQMVCTIDL HQPCLLLYPL PEWEIIEQKL
     SRLSSMNPAE RRVQRLLLGH ASECQMDGAG RLLIAGTLRQ HAGLNKEVML VGQFNKFELW
     DEQTWYQQVK DDIDAEQSTQ EPLSERLQDL SL