Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0C093

- SLMA_ECOLI

UniProt

P0C093 - SLMA_ECOLI

Protein

Nucleoid occlusion factor SlmA

Gene

slmA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (16 Aug 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.3 PublicationsUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi33 – 5220H-T-H motifUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: EcoCyc
    2. identical protein binding Source: IntAct
    3. protein binding Source: EcoCyc
    4. sequence-specific DNA binding Source: EcoCyc

    GO - Biological processi

    1. barrier septum site selection Source: EcoliWiki
    2. negative regulation of barrier septum assembly Source: EcoliWiki
    3. negative regulation of protein polymerization Source: EcoCyc
    4. positive regulation of GTPase activity Source: EcoliWiki

    Keywords - Biological processi

    Cell cycle, Cell division

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11191-MONOMER.
    ECOL316407:JW5641-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleoid occlusion factor SlmAUniRule annotation
    Alternative name(s):
    Protein Ttk
    Synthetically lethal with a defective Min system protein A
    Gene namesi
    Name:slmAUniRule annotation
    Synonyms:ttk, yicB
    Ordered Locus Names:b3641, JW5641
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11191. slmA.

    Subcellular locationi

    Cytoplasmnucleoid 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. bacterial nucleoid Source: EcoCyc
    2. cytoplasm Source: UniProtKB-HAMAP

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi33 – 331T → A: Does not associate with DNA, but can inhibit division when overproduced. 1 Publication
    Mutagenesisi73 – 731R → D: Loss of activity. Binds DNA, but does not associate with FtsZ polymers. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 198198Nucleoid occlusion factor SlmAPRO_0000198966Add
    BLAST

    Proteomic databases

    PaxDbiP0C093.
    PRIDEiP0C093.

    Expressioni

    Gene expression databases

    GenevestigatoriP0C093.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with FtsZ.3 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-8520580,EBI-8520580

    Protein-protein interaction databases

    IntActiP0C093. 1 interaction.
    MINTiMINT-8092383.
    STRINGi511145.b3641.

    Structurei

    Secondary structure

    1
    198
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 2413
    Helixi34 – 407
    Helixi45 – 495
    Helixi55 – 8026
    Helixi84 – 10118
    Helixi103 – 1097
    Helixi122 – 14120
    Turni142 – 1465
    Helixi155 – 17420
    Turni175 – 1784
    Turni182 – 1854
    Helixi186 – 1949

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NXCX-ray2.50A1-198[»]
    ProteinModelPortaliP0C093.
    SMRiP0C093. Positions 9-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 7061HTH tetR-typeUniRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili117 – 14428UniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the nucleoid occlusion factor SlmA family.UniRule annotation
    Contains 1 HTH tetR-type DNA-binding domain.UniRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG1309.
    HOGENOMiHOG000266053.
    KOiK05501.
    OMAiEKDTSAR.
    OrthoDBiEOG6G7R3C.
    PhylomeDBiP0C093.

    Family and domain databases

    Gene3Di1.10.357.10. 1 hit.
    HAMAPiMF_01839. NO_factor_SlmA.
    InterProiIPR023772. 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]
    PfamiPF00440. TetR_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 1 hit.
    SSF48498. SSF48498. 1 hit.
    PROSITEiPS01081. HTH_TETR_1. 1 hit.
    PS50977. HTH_TETR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0C093-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEKQTAKRN RREEILQSLA LMLESSDGSQ RITTAKLAAS VGVSEAALYR    50
    HFPSKTRMFD SLIEFIEDSL ITRINLILKD EKDTTARLRL IVLLLLGFGE 100
    RNPGLTRILT GHALMFEQDR LQGRINQLFE RIEAQLRQVL REKRMREGEG 150
    YTTDETLLAS QILAFCEGML SRFVRSEFKY RPTDDFDARW PLIAAQLQ 198
    Length:198
    Mass (Da):22,836
    Last modified:August 16, 2005 - v1
    Checksum:iC797B0E2875B0E39
    GO

    Sequence cautioni

    The sequence AAA61994.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti196 – 1983QLQ → SCSNMTPDDFSSGEFL in CAA25860. (PubMed:6139280)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqiNP_418098.4. NC_000913.3.
    YP_491792.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76665; AAC76665; b3641.
    BAE77651; BAE77651; BAE77651.
    GeneIDi12930420.
    948158.
    KEGGiecj:Y75_p3533.
    eco:b3641.
    PATRICi32122769. VBIEscCol129921_3761.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    RefSeqi NP_418098.4. NC_000913.3.
    YP_491792.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3NXC X-ray 2.50 A 1-198 [» ]
    ProteinModelPortali P0C093.
    SMRi P0C093. Positions 9-198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0C093. 1 interaction.
    MINTi MINT-8092383.
    STRINGi 511145.b3641.

    Proteomic databases

    PaxDbi P0C093.
    PRIDEi P0C093.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76665 ; AAC76665 ; b3641 .
    BAE77651 ; BAE77651 ; BAE77651 .
    GeneIDi 12930420.
    948158.
    KEGGi ecj:Y75_p3533.
    eco:b3641.
    PATRICi 32122769. VBIEscCol129921_3761.

    Organism-specific databases

    EchoBASEi EB1177.
    EcoGenei EG11191. slmA.

    Phylogenomic databases

    eggNOGi COG1309.
    HOGENOMi HOG000266053.
    KOi K05501.
    OMAi EKDTSAR.
    OrthoDBi EOG6G7R3C.
    PhylomeDBi P0C093.

    Enzyme and pathway databases

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

    Miscellaneous databases

    PROi P0C093.

    Gene expression databases

    Genevestigatori P0C093.

    Family and domain databases

    Gene3Di 1.10.357.10. 1 hit.
    HAMAPi MF_01839. NO_factor_SlmA.
    InterProi 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 ]
    Pfami PF00440. TetR_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 1 hit.
    SSF48498. SSF48498. 1 hit.
    PROSITEi PS01081. HTH_TETR_1. 1 hit.
    PS50977. HTH_TETR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiSLMA_ECOLI
    AccessioniPrimary (citable) accession number: P0C093
    Secondary accession number(s): P06969, Q2M7V5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: August 16, 2005
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Inhibitory activity is enhanced by sequence-specific DNA binding.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3