ID   MRAZ_HERAR              Reviewed;         142 AA.
AC   A4G8U7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Transcriptional regulator MraZ;
GN   Name=mraZ {ECO:0000255|HAMAP-Rule:MF_01008}; OrderedLocusNames=HEAR2820;
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1;
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.-C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
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; CU207211; CAL62934.1; -; Genomic_DNA.
DR   RefSeq; WP_011872190.1; NC_009138.1.
DR   AlphaFoldDB; A4G8U7; -.
DR   SMR; A4G8U7; -.
DR   STRING; 204773.HEAR2820; -.
DR   EnsemblBacteria; CAL62934; CAL62934; HEAR2820.
DR   KEGG; har:HEAR2820; -.
DR   eggNOG; COG2001; Bacteria.
DR   HOGENOM; CLU_107907_2_1_4; -.
DR   OMA; RGQERCL; -.
DR   OrthoDB; 1684767at2; -.
DR   Proteomes; UP000006697; 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; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..142
FT                   /note="Transcriptional regulator MraZ"
FT                   /id="PRO_1000062882"
FT   DOMAIN          5..51
FT                   /note="SpoVT-AbrB 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01076"
FT   DOMAIN          77..120
FT                   /note="SpoVT-AbrB 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01076"
SQ   SEQUENCE   142 AA;  15772 MW;  1EFF37D9EB619462 CRC64;
     MFQGASSLNL DAKGRMTIPA RHRDALLLQC EGRITLTKHP DGCLLLFPRP VWEMRREEIA
     KWPISARAWQ RIFLGNASDV DFDGAGRILI APELRTAAGL TRDVMMMGMG GHFEIWDAAR
     LAESESDAIA AGMPDVLNDF SF