ID SLMA_ECOLI Reviewed; 198 AA.
AC P0C093; P06969; Q2M7V5;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 24-JAN-2024, entry version 145.
DE RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839};
DE AltName: Full=Protein Ttk;
DE AltName: Full=Synthetically lethal with a defective Min system protein A;
GN Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839}; Synonyms=ttk, yicB;
GN OrderedLocusNames=b3641, JW5641;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6139280; DOI=10.1002/j.1460-2075.1983.tb01529.x;
RA Lundberg L.G., Thoresson H.-O., Karlstroem O.H., Nyman P.O.;
RT "Nucleotide sequence of the structural gene for dUTPase of Escherichia coli
RT K-12.";
RL EMBO J. 2:967-971(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP GENE NAME.
RX PubMed=2830228; DOI=10.1128/jb.170.3.1069-1075.1988;
RA El-Hajj H.H., Zhang H., Weiss B.;
RT "Lethality of a dut (deoxyuridine triphosphatase) mutation in Escherichia
RT coli.";
RL J. Bacteriol. 170:1069-1075(1988).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FTSZ.
RX PubMed=15916962; DOI=10.1016/j.molcel.2005.04.012;
RA Bernhardt T.G., de Boer P.A.J.;
RT "SlmA, a nucleoid-associated, ftsZ binding protein required for blocking
RT septal ring assembly over chromosomes in E. coli.";
RL Mol. Cell 18:555-564(2005).
RN [7]
RP FUNCTION, DNA-BINDING, INTERACTION WITH FTSZ, REGULATION OF ACTIVITY, AND
RP MUTAGENESIS OF THR-33 AND ARG-73.
RX PubMed=21321206; DOI=10.1073/pnas.1018674108;
RA Cho H., McManus H.R., Dove S.L., Bernhardt T.G.;
RT "Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization
RT antagonist.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:3773-3778(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, DNA-BINDING, SUBUNIT, AND
RP INTERACTION WITH FTSZ.
RX PubMed=21113127; DOI=10.1038/emboj.2010.288;
RA Tonthat N.K., Arold S.T., Pickering B.F., Van Dyke M.W., Liang S., Lu Y.,
RA Beuria T.K., Margolin W., Schumacher M.A.;
RT "Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps
RT cytokinesis in check.";
RL EMBO J. 30:154-164(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, ECO:0000269|PubMed:15916962,
CC ECO:0000269|PubMed:21113127, ECO:0000269|PubMed:21321206}.
CC -!- SUBUNIT: Homodimer. Interacts with FtsZ. {ECO:0000255|HAMAP-
CC Rule:MF_01839, ECO:0000269|PubMed:15916962,
CC ECO:0000269|PubMed:21113127, ECO:0000269|PubMed:21321206}.
CC -!- INTERACTION:
CC P0C093; P0C093: slmA; NbExp=2; IntAct=EBI-8520580, EBI-8520580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP-
CC Rule:MF_01839, ECO:0000269|PubMed:15916962}.
CC -!- MISCELLANEOUS: Inhibitory activity is enhanced by sequence-specific DNA
CC binding.
CC -!- SIMILARITY: Belongs to the nucleoid occlusion factor SlmA family.
CC {ECO:0000255|HAMAP-Rule:MF_01839}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA61994.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X01714; CAA25860.1; -; Genomic_DNA.
DR EMBL; V01578; CAA24898.1; -; Genomic_DNA.
DR EMBL; V01498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L10328; AAA61994.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76665.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77651.1; -; Genomic_DNA.
DR RefSeq; NP_418098.4; NC_000913.3.
DR RefSeq; WP_000818601.1; NZ_STEB01000024.1.
DR PDB; 3NXC; X-ray; 2.50 A; A=1-198.
DR PDB; 5HBU; X-ray; 2.60 A; A/B/C/D/E/F/G/H=7-198.
DR PDB; 5K58; X-ray; 2.77 A; A/B/E/F=9-198.
DR PDBsum; 3NXC; -.
DR PDBsum; 5HBU; -.
DR PDBsum; 5K58; -.
DR AlphaFoldDB; P0C093; -.
DR SMR; P0C093; -.
DR BioGRID; 4259414; 442.
DR IntAct; P0C093; 1.
DR MINT; P0C093; -.
DR STRING; 511145.b3641; -.
DR jPOST; P0C093; -.
DR PaxDb; 511145-b3641; -.
DR EnsemblBacteria; AAC76665; AAC76665; b3641.
DR GeneID; 75202210; -.
DR GeneID; 948158; -.
DR KEGG; ecj:JW5641; -.
DR KEGG; eco:b3641; -.
DR PATRIC; fig|1411691.4.peg.3065; -.
DR EchoBASE; EB1177; -.
DR eggNOG; COG1309; Bacteria.
DR HOGENOM; CLU_069356_5_0_6; -.
DR InParanoid; P0C093; -.
DR OMA; IEQTVFG; -.
DR OrthoDB; 9179041at2; -.
DR PhylomeDB; P0C093; -.
DR BioCyc; EcoCyc:EG11191-MONOMER; -.
DR PRO; PR:P0C093; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043590; C:bacterial nucleoid; IDA:EcoCyc.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0000918; P:division septum site selection; IMP:EcoliWiki.
DR GO; GO:0010974; P:negative regulation of division septum assembly; IDA:EcoliWiki.
DR GO; GO:0032272; P:negative regulation of protein polymerization; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
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 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_0000198966"
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"
FT MUTAGEN 33
FT /note="T->A: Does not associate with DNA, but can inhibit
FT division when overproduced."
FT /evidence="ECO:0000269|PubMed:21321206"
FT MUTAGEN 73
FT /note="R->D: Loss of activity. Binds DNA, but does not
FT associate with FtsZ polymers."
FT /evidence="ECO:0000269|PubMed:21321206"
FT CONFLICT 196..198
FT /note="QLQ -> SCSNMTPDDFSSGEFL (in Ref. 1; CAA25860)"
FT /evidence="ECO:0000305"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:3NXC"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:5HBU"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:3NXC"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:3NXC"
FT HELIX 55..80
FT /evidence="ECO:0007829|PDB:3NXC"
FT HELIX 84..101
FT /evidence="ECO:0007829|PDB:3NXC"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:3NXC"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5HBU"
FT HELIX 122..141
FT /evidence="ECO:0007829|PDB:3NXC"
FT TURN 142..146
FT /evidence="ECO:0007829|PDB:3NXC"
FT HELIX 155..174
FT /evidence="ECO:0007829|PDB:3NXC"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:3NXC"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:3NXC"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:3NXC"
SQ SEQUENCE 198 AA; 22836 MW; C797B0E2875B0E39 CRC64;
MAEKQTAKRN RREEILQSLA LMLESSDGSQ RITTAKLAAS VGVSEAALYR HFPSKTRMFD
SLIEFIEDSL ITRINLILKD EKDTTARLRL IVLLLLGFGE RNPGLTRILT GHALMFEQDR
LQGRINQLFE RIEAQLRQVL REKRMREGEG YTTDETLLAS QILAFCEGML SRFVRSEFKY
RPTDDFDARW PLIAAQLQ
//
