ID SLMA_SALPA Reviewed; 198 AA.
AC Q5PC27;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839};
GN Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839}; OrderedLocusNames=SPA3584;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV79385.1; -; Genomic_DNA.
DR RefSeq; WP_000818595.1; NC_006511.1.
DR AlphaFoldDB; Q5PC27; -.
DR SMR; Q5PC27; -.
DR KEGG; spt:SPA3584; -.
DR HOGENOM; CLU_069356_5_0_6; -.
DR Proteomes; UP000008185; 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 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.
FT CHAIN 1..198
FT /note="Nucleoid occlusion factor SlmA"
FT /id="PRO_0000198978"
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; 22865 MW; 587A5CDF369E25E1 CRC64;
MAEKQTAKRN RREEILQSLA LMLESSDGSQ RITTAKLAAS VGVSEAALYR HFPSKTRMFD
SLIEFIEDSL ITRINLILKD EKDTSTRLRL IVLLILGFGE RNPGLTRILT GHALMFEQDR
LQGRINQLFE RIEAQLRQVL REKRMREGEG YTTDENLLAS QLLAFCEGML SRFVRSEFKY
RPTDDFDARW PLIAAQLQ
//
