UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase

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P11880 (MURF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 139. 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:
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
EC=6.3.2.10

Alternative name(s):
D-alanyl-D-alanine-adding enzyme
UDP-MurNAc-pentapeptide synthetase

Gene names

Name:	murF
Synonyms:	mra
Ordered Locus Names:	b0086, JW0084

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic activity	ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine.
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the MurCDEF family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity Inferred from direct assay Ref.7. Source: EcoliWiki UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 452

452

UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase

PRO_0000101698

Regions

Nucleotide binding

107 – 113

ATP Potential

Natural variations

Natural variant

288

A → T in murF2; temperature-sensitive mutant with low activity.

Experimental info

Sequence conflict

G → A Ref.1

Sequence conflict

G → A Ref.3

Sequence conflict

178

A → R Ref.1

Sequence conflict

178

A → R Ref.3

Secondary structure

452

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P11880 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: B46E2E57BDBBC572
Show »

FASTA

452

47,447

        10         20         30         40         50         60 
MISVTLSQLT DILNGELQGA DITLDAVTTD TRKLTPGCLF VALKGERFDA HDFADQAKAG 

        70         80         90        100        110        120 
GAGALLVSRP LDIDLPQLIV KDTRLAFGEL AAWVRQQVPA RVVALTGSSG KTSVKEMTAA 

       130        140        150        160        170        180 
ILSQCGNTLY TAGNLNNDIG VPMTLLRLTP EYDYAVIELG ANHQGEIAWT VSLTRPEAAL 

       190        200        210        220        230        240 
VNNLAAAHLE GFGSLAGVAK AKGEIFSGLP ENGIAIMNAD NNDWLNWQSV IGSRKVWRFS 

       250        260        270        280        290        300 
PNAANSDFTA TNIHVTSHGT EFTLQTPTGS VDVLLPLPGR HNIANALAAA ALSMSVGATL 

       310        320        330        340        350        360 
DAIKAGLANL KAVPGRLFPI QLAENQLLLD DSYNANVGSM TAAVQVLAEM PGYRVLVVGD 

       370        380        390        400        410        420 
MAELGAESEA CHVQVGEAAK AAGIDRVLSV GKQSHAISTA SGVGEHFADK TALITRLKLL 

       430        440        450 
IAEQQVITIL VKGSRSAAME EVVRALQENG TC

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the murF gene encoding the UDP-MurNAc-pentapeptide synthetase of Escherichia coli." Parquet C., Flouret B., Mengin-Lecreulx D., van Heijenoort J. Nucleic Acids Res. 17:5379-5379(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Kinetic mechanism of the Escherichia coli UDPMurNAc-tripeptide D-alanyl-D-alanine-adding enzyme: use of a glutathione S-transferase fusion." Anderson M.S., Eveland S.S., Onishi H.R., Pompliano D.L. Biochemistry 35:16264-16269(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / MB2884.
[3]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[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], SEQUENCE REVISION TO 61 AND 178. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Conditionally lethal Escherichia coli murein mutants contain point defects that map to regions conserved among murein and folyl poly-gamma-glutamate ligases: identification of a ligase superfamily." Eveland S.S., Pompliano D.L., Anderson M.S. Biochemistry 36:6223-6229(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT MURF2. Strain: CGSC 5990.
[7]	"Purification and characterization of the D-alanyl-D-alanine-adding enzyme from Escherichia coli." Duncan K., van Heijenoort J., Walsh C.T. Biochemistry 29:2379-2386(1990) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 1-15.
[8]	"Crystal structure of Escherichia coli UDPMurNAc-tripeptide D-alanyl-D-alanine-adding enzyme (MurF) at 2.3-A resolution." Yan Y., Munshi S., Leiting B., Anderson M.S., Chrzas J., Chen Z. J. Mol. Biol. 304:435-445(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X15432 Genomic DNA. Translation: CAA33473.1.
X55034 Genomic DNA. Translation: CAA38863.1.
U67891 Genomic DNA. Translation: AAC44657.1.
U00096 Genomic DNA. Translation: AAC73197.1.
AP009048 Genomic DNA. Translation: BAB96654.2.
U67893 Genomic DNA. Translation: AAB60788.1.

PIR

F64730.

RefSeq

NP_414628.1. NC_000913.2.
YP_488391.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GG4	X-ray	2.30	A/B	1-452	[»]

ProteinModelPortal

P11880.

SMR

P11880. Positions 1-447.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10281N.

IntAct

P11880. 11 interactions.

MINT

MINT-1227223.

STRING

511145.b0086.

Proteomic databases

PaxDb

P11880.

PRIDE

P11880.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73197; AAC73197; b0086.
BAB96654; BAB96654; BAB96654.

GeneID

12932648.
944813.

KEGG

ecj:Y75_p0085.
eco:b0086.

PATRIC

32115277. VBIEscCol129921_0090.

Organism-specific databases

EchoBASE

EB0617.

EcoGene

EG10622. murF.

Phylogenomic databases

eggNOG

COG0770.

HOGENOM

HOG000268120.

K01929.

OMA

GNRNNEI.

ProtClustDB

PRK10773.

Enzyme and pathway databases

BioCyc

EcoCyc:UDP-NACMURALGLDAPAALIG-MONOMER.
ECOL316407:JW0084-MONOMER.
MetaCyc:UDP-NACMURALGLDAPAALIG-MONOMER.

SABIO-RK

P11880.

UniPathway

UPA00219.

Gene expression databases

Genevestigator

P11880.

Family and domain databases

Gene3D

3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.

InterPro

IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR005863. UDP-N-AcMur-pentapeptide_synth.
[Graphical view]

PANTHER

PTHR23135:SF3. PTHR23135:SF3. 1 hit.

Pfam

PF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]

SUPFAM

SSF53244. Mur_ligase_C. 1 hit.
SSF53623. Mur_ligase_cen. 1 hit.

TIGRFAMs

TIGR01143. murF. 1 hit.

ProtoNet

Search...

Other

BindingDB

P11880.

ChEMBL

CHEMBL2540.

EvolutionaryTrace

P11880.

Entry information

Entry name

MURF_ECOLI

Accession

Primary (citable) accession number: P11880
Secondary accession number(s): O07100, P77636

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic 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