SLMA_SALPC
ID SLMA_SALPC Reviewed; 198 AA.
AC C0Q1X3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839};
GN Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839}; OrderedLocusNames=SPC_3814;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
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; CP000857; ACN47889.1; -; Genomic_DNA.
DR RefSeq; WP_000818607.1; NC_012125.1.
DR AlphaFoldDB; C0Q1X3; -.
DR SMR; C0Q1X3; -.
DR EnsemblBacteria; ACN47889; ACN47889; SPC_3814.
DR KEGG; sei:SPC_3814; -.
DR HOGENOM; CLU_069356_5_0_6; -.
DR OMA; IEQTVFG; -.
DR Proteomes; UP000001599; 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_1000188399"
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; 22864 MW; A8705CD88048FE8C CRC64;
MAEKQTAKRN RREEILQSLA LMLESSDGSQ RITTAKLAAS VGVSEAALYR HFPSKTRMFD
SLIEFIEDSL ITRINLILKD EKNTSTRLRL IVLLILGFGE RNPGLTRILT GHALMFEQDR
LQGRINQLFE RIEAQLRQVL REKRMREGEG YTTDENLLAS QLLAFCEGML SRFVRSEFKY
RPTDDFDARW PLIAAQLQ