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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
  • DNA repair Source: UniProtKB-KW
  • negative regulation of cell division Source: EcoliWiki
  • negative regulation of cytokinesis Source: CACAO
  • SOS response Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA repair, Septation, SOS response

Enzyme and pathway databases

BioCyciEcoCyc:EG10984-MONOMER.
ECOL316407:JW0941-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.
STRINGi511145.b0958.

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.
OMAiYGFIMRP.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_01179. SulA. 1 hit.
InterProiIPR004596. Cell_div_suppressor_SulA.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF03846. SulA. 1 hit.
[Graphical view]
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.
PATRICi32117135. VBIEscCol129921_0992.

Cross-referencesi

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.

3D structure databases

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

Protein-protein interaction databases

BioGridi4259653. 213 interactors.
DIPiDIP-10945N.
IntActiP0AFZ5. 2 interactors.
STRINGi511145.b0958.

Chemistry databases

ChEMBLiCHEMBL1287594.

Proteomic databases

PaxDbiP0AFZ5.
PRIDEiP0AFZ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74044; AAC74044; b0958.
BAA35716; BAA35716; BAA35716.
GeneIDi947335.
KEGGiecj:JW0941.
eco:b0958.
PATRICi32117135. VBIEscCol129921_0992.

Organism-specific databases

EchoBASEiEB0977.
EcoGeneiEG10984. sulA.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciEcoCyc:EG10984-MONOMER.
ECOL316407:JW0941-MONOMER.

Miscellaneous databases

PROiP0AFZ5.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_01179. SulA. 1 hit.
InterProiIPR004596. Cell_div_suppressor_SulA.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF03846. SulA. 1 hit.
[Graphical view]
PIRSFiPIRSF003093. SulA. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00623. sula. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSULA_ECOLI
AccessioniPrimary (citable) accession number: P0AFZ5
Secondary accession number(s): P03840, P08846, P71224
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 30, 2016
This is version 98 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.