ID   SLMA_YERPB              Reviewed;         198 AA.
AC   B2JYN0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839};
GN   Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839}; OrderedLocusNames=YPTS_0045;
OS   Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB1/+;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL   Submitted (APR-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; CP001048; ACC87044.1; -; Genomic_DNA.
DR   RefSeq; WP_002208995.1; NZ_CP009780.1.
DR   AlphaFoldDB; B2JYN0; -.
DR   SMR; B2JYN0; -.
DR   GeneID; 66843561; -.
DR   KEGG; ypb:YPTS_0045; -.
DR   PATRIC; fig|502801.10.peg.3721; -.
DR   OMA; IEQTVFG; -.
DR   BioCyc; YPSE502801:YPTS_RS00230-MON; -.
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_1000188408"
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