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Protein

Cell division inhibitor SulA

Gene

sulA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division. The effect of overexpression of SulA is neutralized by antitoxin CbeA (yeeU) (PubMed:22515815).7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei169Essential for degradation by Lon protease1

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • negative regulation of cell division Source: EcoliWiki
  • negative regulation of cytokinesis Source: CACAO
  • negative regulation of FtsZ-dependent cytokinesis Source: EcoCyc
  • negative regulation of GTPase activity Source: EcoCyc
  • negative regulation of protein polymerization Source: EcoCyc
  • SOS response Source: EcoCyc

Keywordsi

Biological processCell cycle, Cell division, DNA damage, Septation, SOS response

Enzyme and pathway databases

BioCyciEcoCyc:EG10984-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division inhibitor SulA
Gene namesi
Name:sulA
Synonyms:sfiA
Ordered Locus Names:b0958, JW0941
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10984. sulA.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39R → A: No effect on degradation by Lon protease. 1 Publication1
Mutagenesisi62R → A: Loss of degradation by Lon protease. 2 Publications1
Mutagenesisi62R → C, H or S: Loss of activity due to loss of ability to bind to FtsZ. 2 Publications1
Mutagenesisi67L → A: Loss of degradation by Lon protease. 1 Publication1
Mutagenesisi72K → A: No effect on degradation by Lon protease. 1 Publication1
Mutagenesisi75R → A: No effect on degradation by Lon protease. 1 Publication1
Mutagenesisi76E → A: No effect on degradation by Lon protease. 1 Publication1
Mutagenesisi77W → A: Loss of degradation by Lon protease. 1 Publication1
Mutagenesisi83L → R: Loss of activity due to loss of ability to bind to FtsZ. 1 Publication1
Mutagenesisi87K → A: Loss of degradation by Lon protease. 1 Publication1
Mutagenesisi98H → A: No effect on degradation by Lon protease. 1 Publication1
Mutagenesisi105R → A: No effect on degradation by Lon protease. 1 Publication1
Mutagenesisi108R → A: No effect on degradation by Lon protease. 1 Publication1
Mutagenesisi115V → A: No effect on degradation by Lon protease. 1 Publication1
Mutagenesisi117G → A: No effect on degradation by Lon protease. 1 Publication1
Mutagenesisi126E → A: No effect on degradation by Lon protease. 1 Publication1
Mutagenesisi128H → A: No effect on degradation by Lon protease. 1 Publication1
Mutagenesisi163I → A: Slight decrease in degradation by Lon protease. 1 Publication1
Mutagenesisi164H → A: No effect on degradation by Lon protease. 1 Publication1
Mutagenesisi167L → A: Slight decrease in degradation by Lon protease. 1 Publication1
Mutagenesisi169H → A: Great decrease in degradation by Lon protease. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1287594.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000723051 – 169Cell division inhibitor SulAAdd BLAST169

Post-translational modificationi

Is rapidly cleaved and degraded by the Lon protease once DNA damage is repaired.4 Publications

Proteomic databases

PaxDbiP0AFZ5.
PRIDEiP0AFZ5.

Expressioni

Inductioni

By DNA damage, as part of the SOS response, repressed by LexA (PubMed:3297925). Induced 8-fold by hydroxyurea (at protein level) (PubMed:20005847).2 Publications

Interactioni

Subunit structurei

Interacts with FtsZ.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
hslUP0A6H55EBI-2012039,EBI-369317

Protein-protein interaction databases

BioGridi4259653. 213 interactors.
DIPiDIP-10945N.
IntActiP0AFZ5. 2 interactors.
STRINGi316385.ECDH10B_1028.

Structurei

3D structure databases

ProteinModelPortaliP0AFZ5.
SMRiP0AFZ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni106 – 112FtsZ bindingBy similarity7
Regioni162 – 169Lon protease binding8

Sequence similaritiesi

Belongs to the SulA family.Curated

Phylogenomic databases

eggNOGiENOG4108ZD2. Bacteria.
COG5404. LUCA.
HOGENOMiHOG000290470.
KOiK13053.

Family and domain databases

HAMAPiMF_01179. SulA. 1 hit.
InterProiView protein in InterPro
IPR004596. Cell_div_suppressor_SulA.
IPR027417. P-loop_NTPase.
PfamiView protein in Pfam
PF03846. SulA. 1 hit.
PIRSFiPIRSF003093. SulA. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00623. sula. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AFZ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYTSGYAHRS SSFSSAASKI ARVSTENTTA GLISEVVYRE DQPMMTQLLL
60 70 80 90 100
LPLLQQLGQQ SRWQLWLTPQ QKLSREWVQA SGLPLTKVMQ ISQLSPCHTV
110 120 130 140 150
ESMVRALRTG NYSVVIGWLA DDLTEEEHAE LVDAANEGNA MGFIMRPVSA
160
SSHATRQLSG LKIHSNLYH
Length:169
Mass (Da):18,801
Last modified:December 20, 2005 - v1
Checksum:iC76B4493773C77C2
GO

Sequence cautioni

The sequence CAA23587 differs from that shown. Reason: Frameshift at position 145.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00307 Genomic DNA. Translation: CAA23587.1. Frameshift.
U00096 Genomic DNA. Translation: AAC74044.1.
AP009048 Genomic DNA. Translation: BAA35716.1.
V00358 Genomic DNA. Translation: CAA23654.1.
PIRiA29016. QQECA1.
RefSeqiNP_415478.1. NC_000913.3.
WP_000288710.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74044; AAC74044; b0958.
BAA35716; BAA35716; BAA35716.
GeneIDi947335.
KEGGiecj:JW0941.
eco:b0958.
PATRICifig|1411691.4.peg.1316.

Similar proteinsi

Entry informationi

Entry nameiSULA_ECOLI
AccessioniPrimary (citable) accession number: P0AFZ5
Secondary accession number(s): P03840, P08846, P71224
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: August 30, 2017
This is version 104 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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