Phospho-N-acetylmuramoyl-pentapeptide-transferase

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P0A6W3 (MRAY_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. History...

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

Documents (3) |

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:
Phospho-N-acetylmuramoyl-pentapeptide-transferase
EC=2.7.8.13

Alternative name(s):
UDP-MurNAc-pentapeptide phosphotransferase

Gene names

Name:	mraY
Synonyms:	murX
Ordered Locus Names:	b0087, JW0085

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	360 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan. Ref.6
Catalytic activity	UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. HAMAP MF_00038
Cofactor	Magnesium or manganese.
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00038
Subcellular location	Cell inner membrane; Multi-pass membrane protein Ref.8.
Sequence similarities	Belongs to the glycosyltransferase 4 family. MraY subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Magnesium Manganese
Molecular function	Transferase
Technical term	Complete proteome 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 cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity Inferred from electronic annotation. Source: EC phospho-N-acetylmuramoyl-pentapeptide-transferase activity Inferred from direct assay Ref.6. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 360

360

Phospho-N-acetylmuramoyl-pentapeptide-transferase HAMAP MF_00038

PRO_0000108820

Regions

Topological domain

1 – 18

Periplasmic Ref.7

Transmembrane

19 – 45

Helical HAMAP MF_00038

Topological domain

46 – 76

Cytoplasmic Ref.7

Transmembrane

77 – 90

Helical HAMAP MF_00038

Topological domain

91 – 96

Periplasmic Ref.7

Transmembrane

97 – 113

Helical HAMAP MF_00038

Topological domain

114 – 133

Cytoplasmic Ref.7

Transmembrane

134 – 156

Helical HAMAP MF_00038

Topological domain

157 – 173

Periplasmic Ref.7

Transmembrane

174 – 188

Helical HAMAP MF_00038

Topological domain

189 – 199

Cytoplasmic Ref.7

Transmembrane

200 – 220

Helical HAMAP MF_00038

Topological domain

221 – 238

Periplasmic Ref.7

Transmembrane

239 – 251

Helical HAMAP MF_00038

Topological domain

252 – 270

Cytoplasmic Ref.7

Transmembrane

271 – 284

Helical HAMAP MF_00038

Topological domain

285 – 287

Periplasmic Ref.7

Transmembrane

288 – 299

Helical HAMAP MF_00038

Topological domain

300 – 341

Cytoplasmic Ref.7

Transmembrane

342 – 357

Helical HAMAP MF_00038

Topological domain

358 – 360

Periplasmic Ref.7

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6W3 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: F3550AFA3CD636AE
Show »

FASTA

360

39,875

        10         20         30         40         50         60 
MLVWLAEHLV KYYSGFNVFS YLTFRAIVSL LTALFISLWM GPRMIAHLQK LSFGQVVRND 

        70         80         90        100        110        120 
GPESHFSKRG TPTMGGIMIL TAIVISVLLW AYPSNPYVWC VLVVLVGYGV IGFVDDYRKV 

       130        140        150        160        170        180 
VRKDTKGLIA RWKYFWMSVI ALGVAFALYL AGKDTPATQL VVPFFKDVMP QLGLFYILLA 

       190        200        210        220        230        240 
YFVIVGTGNA VNLTDGLDGL AIMPTVFVAG GFALVAWATG NMNFASYLHI PYLRHAGELV 

       250        260        270        280        290        300 
IVCTAIVGAG LGFLWFNTYP AQVFMGDVGS LALGGALGII AVLLRQEFLL VIMGGVFVVE 

       310        320        330        340        350        360 
TLSVILQVGS FKLRGQRIFR MAPIHHHYEL KGWPEPRVIV RFWIISLMLV LIGLATLKVR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence involving murD and an open reading frame ORF-Y spacing murF and ftsW in Escherichia coli." Ikeda M., Wachi M., Ishino F., Matsuhashi M. Nucleic Acids Res. 18:1058-1058(1990) [PubMed: 2179861] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"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: 1630901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[3]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Phospho-N-acetylmuramoyl-pentapeptide-transferase of Escherichia coli K12. Properties of the membrane-bound and the extracted and partially purified enzyme." Geis A., Plapp R. Biochim. Biophys. Acta 527:414-424(1978) [PubMed: 215212] [Abstract] Cited for: CHARACTERIZATION. Strain: K12.
[6]	"The Escherichia coli mraY gene encoding UDP-N-acetylmuramoyl-pentapeptide: undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide transferase." Ikeda M., Wachi M., Jung H.K., Ishino F., Matsuhashi M. J. Bacteriol. 173:1021-1026(1991) [PubMed: 1846850] [Abstract] Cited for: FUNCTION. Strain: K12.
[7]	"Topological analysis of the mraY protein catalyzing the first membrane step of peptidoglycan synthesis." Bouhss A., Mengin-Lecreulx D., Le Beller D., Van Heijenoort J. Mol. Microbiol. 34:576-585(1999) [PubMed: 10564498] [Abstract] Cited for: TOPOLOGY.
[8]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X51584 Genomic DNA. Translation: CAA35932.1. X55034 Genomic DNA. Translation: CAA38864.1. U00096 Genomic DNA. Translation: AAC73198.1. AP009048 Genomic DNA. Translation: BAB96655.1.
PIR	S08395.
RefSeq	NP_414629.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P0A6W3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000004236; EBESCP00000004236; EBESCG00000003457. EBESCT00000004237; EBESCP00000004237; EBESCG00000003457. EBESCT00000004238; EBESCP00000004238; EBESCG00000003457. EBESCT00000004239; EBESCP00000004239; EBESCG00000003457. EBESCT00000015389; EBESCP00000014680; EBESCG00000014449.
GeneID	944814.
GenomeReviews	Gene locus JW0085 in contig AP009048_GR. Gene locus b0087 in contig U00096_GR.
KEGG	ecj:JW0085. eco:b0087.
PATRIC	32115279. VBIEscCol129921_0091.
Organism-specific databases
EchoBASE	EB0599.
EcoGene	EG10604. mraY.
Phylogenomic databases
eggNOG	COG0472.
GeneTree	EBGT00050000009109.
HOGENOM	HBG708263.
OMA	RFWIISM.
PhylomeDB	P0A6W3.
ProtClustDB	PRK00108.
Enzyme and pathway databases
BioCyc	EcoCyc:PHOSNACMURPENTATRANS-MONOMER. MetaCyc:PHOSNACMURPENTATRANS-MONOMER.
Gene expression databases
Genevestigator	P0A6W3.
Family and domain databases
HAMAP	MF_00038. MraY. [Tree]
InterPro	IPR000715. Glycosyl_transferase_4. IPR003524. PNAcMuramoyl-5peptid_Trfase. IPR018480. PNAcMuramoyl-5peptid_Trfase_CS. [Graphical view]
KO	K01000.
PANTHER	PTHR22926. Glyco_trans_4. 1 hit. PTHR22926:SF3. PNAcPpept_trans. 1 hit.
Pfam	PF00953. Glycos_transf_4. 1 hit. PF10555. MraY_sig1. 1 hit. [Graphical view]
TIGRFAMs	TIGR00445. MraY. 1 hit.
PROSITE	PS01347. MRAY_1. 1 hit. PS01348. MRAY_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MRAY_ECOLI

Accession

Primary (citable) accession number: P0A6W3
Secondary accession number(s): P15876

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	January 25, 2012
This is version 67 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

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents