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Protein

Protein UmuD

Gene

umuD

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

Functioni

Involved in UV protection and mutation. Essential for induced (or SOS) mutagenesis. May modify the DNA replication machinery to allow bypass synthesis across a damaged template.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei24 – 252Cleavage; by autolysis
Active sitei60 – 601For autocatalytic cleavage activity
Active sitei97 – 971For autocatalytic cleavage activity

GO - Molecular functioni

  • DNA binding Source: InterPro
  • DNA-directed DNA polymerase activity Source: EcoCyc
  • serine-type peptidase activity Source: UniProtKB-KW

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • DNA biosynthetic process Source: GOC
  • DNA repair Source: EcoCyc
  • regulation of transcription, DNA-templated Source: InterPro
  • SOS response Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

DNA damage, DNA repair, SOS mutagenesis, SOS response

Enzyme and pathway databases

BioCyciEcoCyc:EG11057-MONOMER.
ECOL316407:JW1172-MONOMER.
MetaCyc:EG11057-MONOMER.
BRENDAi3.4.21.B30. 2026.

Protein family/group databases

MEROPSiS24.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein UmuD (EC:3.4.21.-)
Cleaved into the following chain:
Gene namesi
Name:umuD
Ordered Locus Names:b1183, JW1172
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11057. umuD.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271P → D in umuD1; non-cleavable. 1 Publication
Mutagenesisi65 – 651G → R in umuD44; non-cleavable. 1 Publication
Mutagenesisi92 – 921G → D in umuD77; non-cleavable. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 139139Protein UmuDPRO_0000041988Add
BLAST
Chaini25 – 139115Protein UmuD'PRO_0000027305Add
BLAST

Keywords - PTMi

Autocatalytic cleavage

Expressioni

Gene expression databases

GenevestigatoriP0AG11.

Interactioni

Protein-protein interaction databases

DIPiDIP-29679N.
IntActiP0AG11. 13 interactions.
STRINGi511145.b1183.

Structurei

Secondary structure

1
139
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 445Combined sources
Helixi48 – 503Combined sources
Beta strandi51 – 555Combined sources
Beta strandi58 – 603Combined sources
Helixi62 – 643Combined sources
Beta strandi71 – 755Combined sources
Beta strandi82 – 843Combined sources
Beta strandi85 – 906Combined sources
Beta strandi93 – 1008Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi120 – 1245Combined sources
Beta strandi125 – 13511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AY9X-ray3.00A/B32-139[»]
1I4VNMR-A/B26-139[»]
1UMUX-ray2.50A/B25-137[»]
DisProtiDP00626.
ProteinModelPortaliP0AG11.
SMRiP0AG11. Positions 32-139.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG11.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S24 family.Curated

Phylogenomic databases

eggNOGiCOG1974.
HOGENOMiHOG000232166.
InParanoidiP0AG11.
KOiK03503.
OMAiFMERVSA.
OrthoDBiEOG6JHRHJ.
PhylomeDBiP0AG11.

Family and domain databases

Gene3Di2.10.109.10. 1 hit.
InterProiIPR028360. Peptidase_S24/S26_b-rbn.
IPR006197. Peptidase_S24_LexA.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
[Graphical view]
PfamiPF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSiPR00726. LEXASERPTASE.
SUPFAMiSSF51306. SSF51306. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AG11-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFIKPADLR EIVTFPLFSD LVQCGFPSPA ADYVEQRIDL NQLLIQHPSA
60 70 80 90 100
TYFVKASGDS MIDGGISDGD LLIVDSAITA SHGDIVIAAV DGEFTVKKLQ
110 120 130
LRPTVQLIPM NSAYSPITIS SEDTLDVFGV VIHVVKAMR
Length:139
Mass (Da):15,063
Last modified:November 1, 1986 - v1
Checksum:i0681A3FFAC7ED583
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10107 Genomic DNA. Translation: AAA24728.1.
M13387 Genomic DNA. Translation: AAA98073.1.
U00096 Genomic DNA. Translation: AAC74267.1.
AP009048 Genomic DNA. Translation: BAA36030.1.
PIRiA03551. ZWECD.
RefSeqiNP_415701.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC74267; AAC74267; b1183.
BAA36030; BAA36030; BAA36030.
GeneIDi945746.
KEGGiecj:Y75_p1155.
eco:b1183.
PATRICi32117612. VBIEscCol129921_1228.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10107 Genomic DNA. Translation: AAA24728.1.
M13387 Genomic DNA. Translation: AAA98073.1.
U00096 Genomic DNA. Translation: AAC74267.1.
AP009048 Genomic DNA. Translation: BAA36030.1.
PIRiA03551. ZWECD.
RefSeqiNP_415701.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AY9X-ray3.00A/B32-139[»]
1I4VNMR-A/B26-139[»]
1UMUX-ray2.50A/B25-137[»]
DisProtiDP00626.
ProteinModelPortaliP0AG11.
SMRiP0AG11. Positions 32-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29679N.
IntActiP0AG11. 13 interactions.
STRINGi511145.b1183.

Protein family/group databases

MEROPSiS24.003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74267; AAC74267; b1183.
BAA36030; BAA36030; BAA36030.
GeneIDi945746.
KEGGiecj:Y75_p1155.
eco:b1183.
PATRICi32117612. VBIEscCol129921_1228.

Organism-specific databases

EchoBASEiEB1050.
EcoGeneiEG11057. umuD.

Phylogenomic databases

eggNOGiCOG1974.
HOGENOMiHOG000232166.
InParanoidiP0AG11.
KOiK03503.
OMAiFMERVSA.
OrthoDBiEOG6JHRHJ.
PhylomeDBiP0AG11.

Enzyme and pathway databases

BioCyciEcoCyc:EG11057-MONOMER.
ECOL316407:JW1172-MONOMER.
MetaCyc:EG11057-MONOMER.
BRENDAi3.4.21.B30. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AG11.
PROiP0AG11.

Gene expression databases

GenevestigatoriP0AG11.

Family and domain databases

Gene3Di2.10.109.10. 1 hit.
InterProiIPR028360. Peptidase_S24/S26_b-rbn.
IPR006197. Peptidase_S24_LexA.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
[Graphical view]
PfamiPF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSiPR00726. LEXASERPTASE.
SUPFAMiSSF51306. SSF51306. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of the umu operon required for inducible mutagenesis in Escherichia coli."
    Kitagawa Y., Akaboshi E., Shinagawa H., Horii T., Ogawa H., Kato T.
    Proc. Natl. Acad. Sci. U.S.A. 82:4336-4340(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "umuDC and mucAB operons whose products are required for UV light- and chemical-induced mutagenesis: UmuD, MucA, and LexA proteins share homology."
    Perry K.L., Elledge S.J., Mitchell B.B., Marsh L., Walker G.C.
    Proc. Natl. Acad. Sci. U.S.A. 82:4331-4335(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Escherichia coli umuDC mutants: DNA sequence alterations and UmuD cleavage."
    Koch W.H., Ennis D.G., Levine A.S., Woodgate R.
    Mol. Gen. Genet. 233:443-448(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  7. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  8. "Structure of the UmuD' protein and its regulation in response to DNA damage."
    Peat T.S., Frank E., McDonald J.P., Levine A.S., Woodgate R., Hendrickson W.A.
    Nature 380:727-730(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF UMUD'.

Entry informationi

Entry nameiUMUD_ECOLI
AccessioniPrimary (citable) accession number: P0AG11
Secondary accession number(s): P04153
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: May 27, 2015
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

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. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.