Protein UmuD - Escherichia coli (strain K12)

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P0AG11 (UMUD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein UmuD
EC=3.4.21.-

Cleaved into the following chain:

Protein UmuD'

Gene names

Name:	umuD
Ordered Locus Names:	b1183, JW1172

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	139 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Sequence similarities	Belongs to the peptidase S24 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair SOS mutagenesis SOS response
Molecular function	Hydrolase Protease Serine protease
PTM	Autocatalytic cleavage
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from mutant phenotype PubMed 10648540. Source: EcoCyc SOS response Inferred from mutant phenotype PubMed 10648540. Source: EcoCyc proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed DNA polymerase activity Inferred from direct assay PubMed 12450411. Source: EcoCyc serine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 139

139

Protein UmuD

PRO_0000041988

Chain

25 – 139

115

Protein UmuD'

PRO_0000027305

Sites

Active site

For autocatalytic cleavage activity

Active site

For autocatalytic cleavage activity

Site

24 – 25

Cleavage; by autolysis

Experimental info

Mutagenesis

P → D in umuD1; non-cleavable.

Mutagenesis

G → R in umuD44; non-cleavable.

Mutagenesis

G → D in umuD77; non-cleavable.

Secondary structure

139

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AG11 [UniParc].

Last modified November 1, 1986. Version 1.
Checksum: 0681A3FFAC7ED583
Show »

FASTA

139

15,063

        10         20         30         40         50         60 
MLFIKPADLR EIVTFPLFSD LVQCGFPSPA ADYVEQRIDL NQLLIQHPSA TYFVKASGDS 

        70         80         90        100        110        120 
MIDGGISDGD LLIVDSAITA SHGDIVIAAV DGEFTVKKLQ LRPTVQLIPM NSAYSPITIS 

       130 
SEDTLDVFGV VIHVVKAMR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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'.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M10107 Genomic DNA. Translation: AAA24728.1.
M13387 Genomic DNA. Translation: AAA98073.1.
U00096 Genomic DNA. Translation: AAC74267.1.
AP009048 Genomic DNA. Translation: BAA36030.1.

PIR

ZWECD. A03551.

RefSeq

NP_415701.1. NC_000913.2.
YP_489450.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AY9	X-ray	3.00	A/B	32-139	[»]
1I4V	NMR	-	A/B	26-139	[»]
1UMU	X-ray	2.50	A/B	25-137	[»]

ProteinModelPortal

P0AG11.

SMR

P0AG11. Positions 32-139.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29679N.

IntAct

P0AG11. 6 interactions.

STRING

511145.b1183.

Protein family/group databases

MEROPS

S24.003.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74267; AAC74267; b1183.
BAA36030; BAA36030; BAA36030.

GeneID

12932823.
945746.

KEGG

ecj:Y75_p1155.
eco:b1183.

PATRIC

32117612. VBIEscCol129921_1228.

Organism-specific databases

EchoBASE

EB1050.

EcoGene

EG11057. umuD.

Phylogenomic databases

eggNOG

COG1974.

HOGENOM

HOG000232166.

K03503.

OMA

RVSAGFP.

ProtClustDB

PRK10276.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11057-MONOMER.
ECOL316407:JW1172-MONOMER.
MetaCyc:EG11057-MONOMER.

Gene expression databases

Genevestigator

P0AG11.

Family and domain databases

Gene3D

2.10.109.10. 1 hit.

InterPro

IPR006197. Peptidase_S24_LexA.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR011056. Peptidase_S24_S26A/B/C_b-rbn.
[Graphical view]

Pfam

PF00717. Peptidase_S24. 1 hit.
[Graphical view]

PRINTS

PR00726. LEXASERPTASE.

SUPFAM

SSF51306. Pept_S24_S26_C. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0AG11.

Entry information

Entry name

UMUD_ECOLI

Accession

Primary (citable) accession number: P0AG11
Secondary accession number(s): P04153

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	November 1, 1986
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following chain:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents