SLMA_YERPA
ID SLMA_YERPA Reviewed; 198 AA.
AC Q1C264;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839};
GN Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839}; OrderedLocusNames=YPA_3496;
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG15458.1; -; Genomic_DNA.
DR RefSeq; WP_002208995.1; NZ_CP009906.1.
DR AlphaFoldDB; Q1C264; -.
DR SMR; Q1C264; -.
DR EnsemblBacteria; ABG15458; ABG15458; YPA_3496.
DR GeneID; 66843561; -.
DR KEGG; ypa:YPA_3496; -.
DR OMA; IEQTVFG; -.
DR Proteomes; UP000001971; 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_1000070540"
FT DOMAIN 9..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 119..144
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
SQ SEQUENCE 198 AA; 23107 MW; 9E4C5024D8FE5785 CRC64;
MAEKENTKRN RREEILQALA QMLESSDGSQ RITTAKLAAN VGVSEAALYR HFPSKTRMFD
SLIEFIEDSL MSRINLILQD EKETFNRLRL ILLLVLGFAE RNPGLTRIMT GHALMFEQDR
LQGRINQLFE RIEMQLRQVL REKKLRDGQG FIHDEALLAT QLLAFCEGML SRFVRSEFRY
CPTQEFDSRW PLIVAQLQ
