ID SLMA_ECO5E Reviewed; 198 AA. AC B5YWD9; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 11-DEC-2019, entry version 65. DE RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839}; GN Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839}; GN OrderedLocusNames=ECH74115_5011; OS Escherichia coli O157:H7 (strain EC4115 / EHEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=444450; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EC4115 / EHEC; RX PubMed=22135463; DOI=10.1073/pnas.1107176108; RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.; RT "Genomic anatomy of Escherichia coli O157:H7 outbreaks."; RL Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001164; ACI38750.1; -; Genomic_DNA. DR RefSeq; WP_000818601.1; NC_011353.1. DR SMR; B5YWD9; -. DR EnsemblBacteria; ACI38750; ACI38750; ECH74115_5011. DR KEGG; ecf:ECH74115_5011; -. DR HOGENOM; HOG000266053; -. DR KO; K05501; -. DR OMA; IEQTVFG; -. 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_1000188381" 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 //