ID   SLMA_ECODH              Reviewed;         198 AA.
AC   B1X975;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839};
GN   Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839};
GN   OrderedLocusNames=ECDH10B_3823;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/jb.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into the
RT   biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Required for nucleoid occlusion (NO) phenomenon, which
CC       prevents Z-ring formation and cell division over the nucleoid. Acts as
CC       a DNA-associated cell division inhibitor that binds simultaneously
CC       chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers.
CC       SlmA-DNA-binding sequences (SBS) are dispersed on non-Ter regions of
CC       the chromosome, preventing FtsZ polymerization at these regions.
CC       {ECO:0000255|HAMAP-Rule:MF_01839}.
CC   -!- SUBUNIT: Homodimer. Interacts with FtsZ. {ECO:0000255|HAMAP-
CC       Rule:MF_01839}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP-
CC       Rule:MF_01839}.
CC   -!- SIMILARITY: Belongs to the nucleoid occlusion factor SlmA family.
CC       {ECO:0000255|HAMAP-Rule:MF_01839}.
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DR   EMBL; CP000948; ACB04691.1; -; Genomic_DNA.
DR   RefSeq; WP_000818601.1; NC_010473.1.
DR   AlphaFoldDB; B1X975; -.
DR   SMR; B1X975; -.
DR   GeneID; 66672464; -.
DR   KEGG; ecd:ECDH10B_3823; -.
DR   HOGENOM; CLU_069356_5_0_6; -.
DR   OMA; IEQTVFG; -.
DR   BioCyc; ECOL316385:ECDH10B_RS19460-MON; -.
DR   GO; GO:0043590; C:bacterial nucleoid; IEA:UniProtKB-UniRule.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010974; P:negative regulation of division septum assembly; IEA:InterPro.
DR   HAMAP; MF_01839; NO_factor_SlmA; 1.
DR   InterPro; IPR023772; DNA-bd_HTH_TetR-type_CS.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001647; HTH_TetR.
DR   InterPro; IPR023769; NO_SlmA.
DR   InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR   Pfam; PF00440; TetR_N; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF48498; SSF48498; 1.
DR   PROSITE; PS01081; HTH_TETR_1; 1.
DR   PROSITE; PS50977; HTH_TETR_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; DNA-binding.
FT   CHAIN           1..198
FT                   /note="Nucleoid occlusion factor SlmA"
FT                   /id="PRO_1000188385"
FT   DOMAIN          10..70
FT                   /note="HTH tetR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
FT   DNA_BIND        33..52
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
FT   COILED          117..144
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
SQ   SEQUENCE   198 AA;  22836 MW;  C797B0E2875B0E39 CRC64;
     MAEKQTAKRN RREEILQSLA LMLESSDGSQ RITTAKLAAS VGVSEAALYR HFPSKTRMFD
     SLIEFIEDSL ITRINLILKD EKDTTARLRL IVLLLLGFGE RNPGLTRILT GHALMFEQDR
     LQGRINQLFE RIEAQLRQVL REKRMREGEG YTTDETLLAS QILAFCEGML SRFVRSEFKY
     RPTDDFDARW PLIAAQLQ