SLMA_ALIFM
ID SLMA_ALIFM Reviewed; 196 AA.
AC B5FFF4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839};
GN Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839}; OrderedLocusNames=VFMJ11_0121;
OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=388396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ11;
RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT "Complete sequence of Vibrio fischeri strain MJ11.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001139; ACH64955.1; -; Genomic_DNA.
DR RefSeq; WP_005417043.1; NC_011184.1.
DR AlphaFoldDB; B5FFF4; -.
DR SMR; B5FFF4; -.
DR EnsemblBacteria; ACH64955; ACH64955; VFMJ11_0121.
DR GeneID; 64241714; -.
DR KEGG; vfm:VFMJ11_0121; -.
DR HOGENOM; CLU_069356_5_0_6; -.
DR OMA; IEQTVFG; -.
DR Proteomes; UP000001857; Chromosome I.
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; 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; PS50977; HTH_TETR_2; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; DNA-binding.
FT CHAIN 1..196
FT /note="Nucleoid occlusion factor SlmA"
FT /id="PRO_1000188406"
FT DOMAIN 7..68
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
FT DNA_BIND 31..50
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
FT COILED 71..93
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
SQ SEQUENCE 196 AA; 22790 MW; 8F48E4D86C466566 CRC64;
MATPRKPNRR DEILQALAEM LESNEGAARI TTAKLAKQVG VSEAALYRHF PSKAKMFEGL
IEFIEESIFS RVNRILEDEK DTLKRIELLL KLLLAFAERN PGLTRIMTGH ALMFENERLR
SRINQIFERI ELQFKQILRE RKLREGKAFP IDESILAAQL VGQVEGSFCR FVRSDFKYQP
TENFNEYWAL LSAQIQ