Nucleoid occlusion factor SlmA - Escherichia coli (strain K12)

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P0C093 (SLMA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Nucleoid occlusion factor SlmA

Alternative name(s):
Protein Ttk
Synthetically lethal with a defective Min system protein A

Gene names

Name:	slmA
Synonyms:	ttk, yicB
Ordered Locus Names:	b3641, JW5641

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for nucleoid occlusion (NO) phenomenon, which prevents Z-ring formation and cell division over the nucleoid. Acts as a DNA-associated cell division inhibitor that binds simultaneously chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers. SlmA-DNA-binding sequences (SBS) are dispersed on non-Ter regions of the chromosome, preventing FtsZ polymerization at these regions. Ref.6 Ref.7 Ref.8
Subunit structure	Homodimer. Interacts with FtsZ. Ref.6 Ref.7 Ref.8
Subcellular location	Cytoplasm › nucleoid Ref.6.
Miscellaneous	Inhibitory activity is enhanced by sequence-specific DNA binding. HAMAP-Rule MF_01839
Sequence similarities	Belongs to the nucleoid occlusion factor SlmA family. Contains 1 HTH tetR-type DNA-binding domain.
Sequence caution	The sequence AAA61994.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm
Domain	Coiled coil
Ligand	DNA-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	barrier septum site selection Inferred from mutant phenotype Ref.6. Source: EcoliWiki cell cycle Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of barrier septum assembly Inferred from direct assay Ref.7. Source: EcoliWiki negative regulation of protein polymerization Inferred from direct assay Ref.7. Source: EcoCyc positive regulation of GTPase activity Inferred from direct assay Ref.7. Source: EcoliWiki
Cellular_component	bacterial nucleoid Inferred from direct assay Ref.6. Source: EcoCyc cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular_function	sequence-specific DNA binding Inferred from direct assay Ref.8 Ref.7. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 198

198

Nucleoid occlusion factor SlmA HAMAP-Rule MF_01839

PRO_0000198966

Regions

Domain

10 – 70

HTH tetR-type

DNA binding

33 – 52

H-T-H motif By similarity

Coiled coil

117 – 144

Potential

Experimental info

Mutagenesis

T → A: Does not associate with DNA, but can inhibit division when overproduced. Ref.7

Mutagenesis

R → D: Loss of activity. Binds DNA, but does not associate with FtsZ polymers. Ref.7

Sequence conflict

196 – 198

QLQ → SCSNMTPDDFSSGEFL in CAA25860. Ref.1

Secondary structure

198

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0C093 [UniParc].

Last modified August 16, 2005. Version 1.
Checksum: C797B0E2875B0E39
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FASTA

198

22,836

        10         20         30         40         50         60 
MAEKQTAKRN RREEILQSLA LMLESSDGSQ RITTAKLAAS VGVSEAALYR HFPSKTRMFD 

        70         80         90        100        110        120 
SLIEFIEDSL ITRINLILKD EKDTTARLRL IVLLLLGFGE RNPGLTRILT GHALMFEQDR 

       130        140        150        160        170        180 
LQGRINQLFE RIEAQLRQVL REKRMREGEG YTTDETLLAS QILAFCEGML SRFVRSEFKY 

       190 
RPTDDFDARW PLIAAQLQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the structural gene for dUTPase of Escherichia coli K-12." Lundberg L.G., Thoresson H.-O., Karlstroem O.H., Nyman P.O. EMBO J. 2:967-971(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R. Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Lethality of a dut (deoxyuridine triphosphatase) mutation in Escherichia coli." El-Hajj H.H., Zhang H., Weiss B. J. Bacteriol. 170:1069-1075(1988) [PubMed] [Europe PMC] [Abstract] Cited for: GENE NAME.
[6]	"SlmA, a nucleoid-associated, ftsZ binding protein required for blocking septal ring assembly over chromosomes in E. coli." Bernhardt T.G., de Boer P.A.J. Mol. Cell 18:555-564(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FTSZ.
[7]	"Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist." Cho H., McManus H.R., Dove S.L., Bernhardt T.G. Proc. Natl. Acad. Sci. U.S.A. 108:3773-3778(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH FTSZ, REGULATION OF ACTIVITY, MUTAGENESIS OF THR-33 AND ARG-73.
[8]	"Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check." Tonthat N.K., Arold S.T., Pickering B.F., Van Dyke M.W., Liang S., Lu Y., Beuria T.K., Margolin W., Schumacher M.A. EMBO J. 30:154-164(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, DNA-BINDING, SUBUNIT, INTERACTION WITH FTSZ.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X01714 Genomic DNA. Translation: CAA25860.1.
V01578 Genomic DNA. Translation: CAA24898.1.
V01498 Genomic DNA. No translation available.
L10328 Genomic DNA. Translation: AAA61994.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76665.2.
AP009048 Genomic DNA. Translation: BAE77651.1.

RefSeq

NP_418098.4. NC_000913.2.
YP_491792.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3NXC	X-ray	2.50	A	1-198	[»]

ProteinModelPortal

P0C093.

SMR

P0C093. Positions 9-198.

ModBase

Search...

Protein-protein interaction databases

STRING

511145.b3641.

Proteomic databases

PaxDb

P0C093.

PRIDE

P0C093.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76665; AAC76665; b3641.
BAE77651; BAE77651; BAE77651.

GeneID

12930420.
948158.

KEGG

ecj:Y75_p3533.
eco:b3641.

PATRIC

32122769. VBIEscCol129921_3761.

Organism-specific databases

EchoBASE

EB1177.

EcoGene

EG11191. slmA.

Phylogenomic databases

eggNOG

COG1309.

HOGENOM

HOG000266053.

K05501.

OMA

RYVRSNF.

ProtClustDB

PRK09480.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11191-MONOMER.
ECOL316407:JW5641-MONOMER.

Gene expression databases

Genevestigator

P0C093.

Family and domain databases

Gene3D

1.10.357.10. 1 hit.

HAMAP

MF_01839. NO_factor_SlmA.

InterPro

IPR023772. DNA-bd_HTH_TetR-type_CS.
IPR009057. Homeodomain-like.
IPR001647. HTH_TetR.
IPR023769. NO_SlmA.
IPR015893. Tet_transcr_reg_TetR-like_C.
IPR011075. Tet_transcr_reg_TetR-rel_C.
[Graphical view]

Pfam

PF00440. TetR_N. 1 hit.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 1 hit.
SSF48498. TetR_like_C. 1 hit.

PROSITE

PS01081. HTH_TETR_1. 1 hit.
PS50977. HTH_TETR_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SLMA_ECOLI

Accession

Primary (citable) accession number: P0C093
Secondary accession number(s): P06969, Q2M7V5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	August 16, 2005
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents