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Protein

Cell division inhibitor SulA

Gene

sulA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

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
STRINGi316385.ECDH10B_1028

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
PATRICifig|1411691.4.peg.1316

Organism-specific databases

EchoBASEiEB0977
EcoGeneiEG10984 sulA

Phylogenomic databases

eggNOGiENOG4108ZD2 Bacteria
COG5404 LUCA
HOGENOMiHOG000290470
KOiK13053

Enzyme and pathway databases

BioCyciEcoCyc:EG10984-MONOMER

Miscellaneous databases

PROiPR:P0AFZ5

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
ProtoNetiSearch...

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: November 7, 2018
This is version 106 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. SIMILARITY comments
    Index of protein domains and families
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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Main funding by: National Institutes of Health

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