ID   SLMA_ECOK1              Reviewed;         198 AA.
AC   A1AHH2;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839};
GN   Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839}; OrderedLocusNames=Ecok1_36180;
GN   ORFNames=APECO1_2820;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ03112.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000468; ABJ03112.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000818598.1; NC_008563.1.
DR   AlphaFoldDB; A1AHH2; -.
DR   SMR; A1AHH2; -.
DR   EnsemblBacteria; ABJ03112; ABJ03112; APECO1_2820.
DR   KEGG; ecv:APECO1_2820; -.
DR   HOGENOM; CLU_069356_5_0_6; -.
DR   Proteomes; UP000008216; Chromosome.
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_0000413758"
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;  22806 MW;  C78D00E2875B1F39 CRC64;
     MAEKQTAKRN RREEILQSLA LMLESSDGSQ RITTAKLAAS VGVSEAALYR HFPSKTRMFD
     SLIEFIEDSL ITRINLILKD EKDTTARLRL IVLLLLGFGE RNPGLTRILT GHALMFEQDR
     LQGRINQLFE RIEAQLRQVL REKRMREGEG YATDETLLAS QILAFCEGML SRFVRSEFKY
     RPTDDFDARW PLIAAQLQ