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Database: UniProt
Entry: Q8ZL46
LinkDB: Q8ZL46
Original site: Q8ZL46 
ID   SLMA_SALTY              Reviewed;         198 AA.
AC   Q8ZL46; Q93V18;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 120.
DE   RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839};
GN   Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839}; OrderedLocusNames=STM3732;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   van der Straaten T., Wesel A., van Dissel J.T.;
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AF233062; AAF64285.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22591.1; -; Genomic_DNA.
DR   RefSeq; NP_462632.1; NC_003197.2.
DR   RefSeq; WP_000818607.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZL46; -.
DR   SMR; Q8ZL46; -.
DR   STRING; 99287.STM3732; -.
DR   PaxDb; 99287-STM3732; -.
DR   GeneID; 1255256; -.
DR   PATRIC; fig|99287.12.peg.3948; -.
DR   HOGENOM; CLU_069356_5_0_6; -.
DR   OMA; IEQTVFG; -.
DR   PhylomeDB; Q8ZL46; -.
DR   BioCyc; SENT99287:STM3732-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0043590; C:bacterial nucleoid; IEA:UniProtKB-UniRule.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
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   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   Gene3D; 1.10.357.10; Tetracycline Repressor, domain 2; 1.
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   PANTHER; PTHR30055; HTH-TYPE TRANSCRIPTIONAL REGULATOR RUTR; 1.
DR   PANTHER; PTHR30055:SF183; NUCLEOID OCCLUSION FACTOR SLMA; 1.
DR   Pfam; PF00440; TetR_N; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF48498; Tetracyclin repressor-like, C-terminal domain; 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;
KW   Reference proteome.
FT   CHAIN           1..198
FT                   /note="Nucleoid occlusion factor SlmA"
FT                   /id="PRO_0000198980"
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"
FT   CONFLICT        83..86
FT                   /note="NTST -> DTTA (in Ref. 1; AAF64285)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="I -> L (in Ref. 1; AAF64285)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156
FT                   /note="N -> T (in Ref. 1; AAF64285)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="L -> I (in Ref. 1; AAF64285)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196..198
FT                   /note="QLQ -> SCSNMTPDDFSSGEFL (in Ref. 1; AAF64285)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   198 AA;  22864 MW;  A8705CD88048FE8C CRC64;
     MAEKQTAKRN RREEILQSLA LMLESSDGSQ RITTAKLAAS VGVSEAALYR HFPSKTRMFD
     SLIEFIEDSL ITRINLILKD EKNTSTRLRL IVLLILGFGE RNPGLTRILT GHALMFEQDR
     LQGRINQLFE RIEAQLRQVL REKRMREGEG YTTDENLLAS QLLAFCEGML SRFVRSEFKY
     RPTDDFDARW PLIAAQLQ
//
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