SLMA_MARN8
ID SLMA_MARN8 Reviewed; 195 AA.
AC A1U6F3;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839};
GN Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839}; OrderedLocusNames=Maqu_3502;
OS Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS aquaeolei).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=351348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX PubMed=21335390; DOI=10.1128/aem.01866-10;
RA Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA Edwards K.J.;
RT "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT 'opportunitroph'.";
RL Appl. Environ. Microbiol. 77:2763-2771(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; CP000514; ABM20572.1; -; Genomic_DNA.
DR RefSeq; WP_011786913.1; NC_008740.1.
DR AlphaFoldDB; A1U6F3; -.
DR SMR; A1U6F3; -.
DR STRING; 351348.Maqu_3502; -.
DR EnsemblBacteria; ABM20572; ABM20572; Maqu_3502.
DR KEGG; maq:Maqu_3502; -.
DR eggNOG; COG1309; Bacteria.
DR HOGENOM; CLU_069356_5_0_6; -.
DR OMA; IEQTVFG; -.
DR OrthoDB; 1437290at2; -.
DR Proteomes; UP000000998; 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; 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..195
FT /note="Nucleoid occlusion factor SlmA"
FT /id="PRO_0000413760"
FT DOMAIN 6..66
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
FT DNA_BIND 29..48
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
FT COILED 118..138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
SQ SEQUENCE 195 AA; 22100 MW; BBEA1423E0A8A7C3 CRC64;
MTNQKPSRRE SILQALVELL QSDPGARITT AGLAKTVGVT EAALYRHFPS KRKMFEALIE
FAEEAVFSRC QVILQEQEDV RVRLQQLSHL VLVFAERNPG LCCVLTGDAL MGEDESLRKR
ASQFFERLET QIRQALKEGE IRQGLRPRTT AARGADFVMV FVEGRIQRFV RSSFLRLPTS
DFDEAWGLVS EAVWG