ID   SLMA_KLEP7              Reviewed;         198 AA.
AC   A6TFN2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839};
GN   Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839};
GN   OrderedLocusNames=KPN78578_39420; ORFNames=KPN_03981;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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; CP000647; ABR79366.1; -; Genomic_DNA.
DR   RefSeq; WP_002922598.1; NC_009648.1.
DR   PDB; 5HSZ; X-ray; 2.30 A; A/B=3-198.
DR   PDBsum; 5HSZ; -.
DR   AlphaFoldDB; A6TFN2; -.
DR   SMR; A6TFN2; -.
DR   STRING; 272620.KPN_03981; -.
DR   EnsemblBacteria; ABR79366; ABR79366; KPN_03981.
DR   KEGG; kpn:KPN_03981; -.
DR   HOGENOM; CLU_069356_5_0_6; -.
DR   OMA; IEQTVFG; -.
DR   Proteomes; UP000000265; 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   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   DNA-binding; Reference proteome.
FT   CHAIN           1..198
FT                   /note="Nucleoid occlusion factor SlmA"
FT                   /id="PRO_1000070522"
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..145
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
FT   TURN            4..8
FT                   /evidence="ECO:0007829|PDB:5HSZ"
FT   HELIX           10..24
FT                   /evidence="ECO:0007829|PDB:5HSZ"
FT   HELIX           26..29
FT                   /evidence="ECO:0007829|PDB:5HSZ"
FT   HELIX           34..40
FT                   /evidence="ECO:0007829|PDB:5HSZ"
FT   HELIX           45..51
FT                   /evidence="ECO:0007829|PDB:5HSZ"
FT   HELIX           55..80
FT                   /evidence="ECO:0007829|PDB:5HSZ"
FT   HELIX           84..101
FT                   /evidence="ECO:0007829|PDB:5HSZ"
FT   HELIX           103..109
FT                   /evidence="ECO:0007829|PDB:5HSZ"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:5HSZ"
FT   HELIX           119..141
FT                   /evidence="ECO:0007829|PDB:5HSZ"
FT   HELIX           143..147
FT                   /evidence="ECO:0007829|PDB:5HSZ"
FT   HELIX           155..175
FT                   /evidence="ECO:0007829|PDB:5HSZ"
FT   TURN            176..178
FT                   /evidence="ECO:0007829|PDB:5HSZ"
FT   TURN            182..185
FT                   /evidence="ECO:0007829|PDB:5HSZ"
FT   HELIX           186..196
FT                   /evidence="ECO:0007829|PDB:5HSZ"
SQ   SEQUENCE   198 AA;  22824 MW;  A34BBCB2C54023AA CRC64;
     MAEKQTAKRN RREEILQSLA LMLESSDGSQ RITTAKLAAS VGVSEAALYR HFPSKTRMFD
     SLIEFIEDSL ITRINLILKD EKDTTARLRL IVLLILGFGE RNPGLTRILT GHALMFEQDR
     LQGRINQLFE RIEAQLRQVM REKKMREGEG YTLDETLLAS QLLAFCEGML SRFVRSEFKY
     RPTDDFDARW PLVAAQLQ