ID   SLMA_KLEP3              Reviewed;         198 AA.
AC   B5XTG2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839};
GN   Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839}; OrderedLocusNames=KPK_0113;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI06851.1; -; Genomic_DNA.
DR   PDB; 4GCK; X-ray; 2.05 A; A/B/C/D=1-198.
DR   PDB; 4GFL; X-ray; 2.30 A; A/B=1-198.
DR   PDBsum; 4GCK; -.
DR   PDBsum; 4GFL; -.
DR   AlphaFoldDB; B5XTG2; -.
DR   SMR; B5XTG2; -.
DR   EnsemblBacteria; ACI06851; ACI06851; KPK_0113.
DR   KEGG; kpe:KPK_0113; -.
DR   HOGENOM; CLU_069356_5_0_6; -.
DR   OMA; IEQTVFG; -.
DR   OrthoDB; 1437290at2; -.
DR   Proteomes; UP000001734; 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.
FT   CHAIN           1..198
FT                   /note="Nucleoid occlusion factor SlmA"
FT                   /id="PRO_1000188391"
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          119..144
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01839"
FT   HELIX           10..24
FT                   /evidence="ECO:0007829|PDB:4GCK"
FT   HELIX           26..29
FT                   /evidence="ECO:0007829|PDB:4GCK"
FT   HELIX           34..41
FT                   /evidence="ECO:0007829|PDB:4GCK"
FT   HELIX           45..51
FT                   /evidence="ECO:0007829|PDB:4GCK"
FT   HELIX           55..80
FT                   /evidence="ECO:0007829|PDB:4GCK"
FT   HELIX           84..101
FT                   /evidence="ECO:0007829|PDB:4GCK"
FT   HELIX           103..109
FT                   /evidence="ECO:0007829|PDB:4GCK"
FT   HELIX           113..116
FT                   /evidence="ECO:0007829|PDB:4GCK"
FT   HELIX           119..147
FT                   /evidence="ECO:0007829|PDB:4GCK"
FT   HELIX           155..175
FT                   /evidence="ECO:0007829|PDB:4GCK"
FT   TURN            176..178
FT                   /evidence="ECO:0007829|PDB:4GCK"
FT   TURN            182..185
FT                   /evidence="ECO:0007829|PDB:4GCK"
FT   HELIX           186..194
FT                   /evidence="ECO:0007829|PDB:4GCK"
SQ   SEQUENCE   198 AA;  22866 MW;  BC44ACAC8F5023AA CRC64;
     MAEKQTAKRN RREEILQSLA LMLESSDGSQ RITTAKLAAS VGVSEAALYR HFPSKTRMFD
     SLIEFIEDSL ITRINLILKD EKDTTARLRL IVLLILGFGE RNPGLTRILT GHALMFEQDR
     LQGRINQLFE RIEVQLRQVM REKKMREGEG YTLDETLLAS QLLAFCEGML SRFVRSEFKY
     RPTDDFEARW PLVAAQLQ