ID   MRAZ_ECOL5              Reviewed;         152 AA.
AC   Q0TLQ8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Transcriptional regulator MraZ;
GN   Name=mraZ {ECO:0000255|HAMAP-Rule:MF_01008}; OrderedLocusNames=ECP_0083;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG68123.1; -; Genomic_DNA.
DR   RefSeq; WP_001295770.1; NC_008253.1.
DR   AlphaFoldDB; Q0TLQ8; -.
DR   SMR; Q0TLQ8; -.
DR   STRING; 362663.ECP_0083; -.
DR   EnsemblBacteria; ABG68123; ABG68123; ECP_0083.
DR   GeneID; 66671629; -.
DR   KEGG; ecp:ECP_0083; -.
DR   HOGENOM; CLU_107907_2_0_6; -.
DR   OMA; RGQERCL; -.
DR   Proteomes; UP000009182; 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_1000062873"
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;  17360 MW;  48277D972BEDC765 CRC64;
     MFRGATLVNL DSKGRLSVPT RYREQLLENA AGQMVCTIDI HHPCLLLYPL PEWEIIEQKL
     SRLSSMNPVE RRVQRLLLGH ASECQMDGAG RLLIAPVLRQ HAGLTKEVML VGQFNKFELW
     DETTWHQQVK EDIDAEQLAT GDLSERLQDL SL