MRAZ_PECCP
ID MRAZ_PECCP Reviewed; 152 AA.
AC C6DEV2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Transcriptional regulator MraZ;
GN Name=mraZ {ECO:0000255|HAMAP-Rule:MF_01008}; OrderedLocusNames=PC1_3601;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT14616.1; -; Genomic_DNA.
DR RefSeq; WP_015841733.1; NC_012917.1.
DR AlphaFoldDB; C6DEV2; -.
DR SMR; C6DEV2; -.
DR STRING; 561230.PC1_3601; -.
DR EnsemblBacteria; ACT14616; ACT14616; PC1_3601.
DR KEGG; pct:PC1_3601; -.
DR eggNOG; COG2001; Bacteria.
DR HOGENOM; CLU_107907_2_0_6; -.
DR OMA; RGQERCL; -.
DR OrthoDB; 1684767at2; -.
DR Proteomes; UP000002736; 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_1000213180"
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; 17599 MW; AFD84AC59790724C CRC64;
MFRGATLVNL DSKGRLAVPT RYREMLNGES QGQMVCTIDL HQPCLLLYPL PEWEIIEQKL
SRLSSMNPAE RRVQRLLLGH ASECQMDSAG RLLIANTLRQ HADLKKEVML VGQFNKFELW
DEQTWYQQVR DDIDAEQSTQ EPLSDRLQDL SL