ID   MRAZ_SALPA              Reviewed;         152 AA.
AC   Q5PDH5;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Transcriptional regulator MraZ;
GN   Name=mraZ {ECO:0000255|HAMAP-Rule:MF_01008}; OrderedLocusNames=SPA0121;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV76154.1; -; Genomic_DNA.
DR   RefSeq; WP_000488297.1; NC_006511.1.
DR   AlphaFoldDB; Q5PDH5; -.
DR   SMR; Q5PDH5; -.
DR   EnsemblBacteria; AAV76154; AAV76154; SPA0121.
DR   KEGG; spt:SPA0121; -.
DR   HOGENOM; CLU_107907_2_0_6; -.
DR   OMA; RGQERCL; -.
DR   Proteomes; UP000008185; 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_0000108530"
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;  17454 MW;  4EDFF9A787E809F5 CRC64;
     MFRGATLVNL DSKGRLTVPT RYREQLIESA TGQMVCTIDI HRPCLLLYPL PEWEIIEQKL
     SRLSSMNPVE RRVQRLLLGH ASECQMDGAG RLLIAPVLRQ HAGLTKEVML VGQFNKFELW
     DETTWYQQVK EDIDAEQSAT ETLSERLQDL SL