Phospho-N-acetylmuramoyl-pentapeptide-transferase

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Reviewed, UniProtKB/Swiss-Prot P0A6W3 (MRAY_ECOLI)

Last modified February 9, 2010. Version 51. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

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

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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. HAMAP MF_00038
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.

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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
Ligand	Magnesium Manganese
Molecular function	Transferase
Technical term	Complete 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-SubCell plasma membrane Inferred from electronic annotation. Source: HAMAP
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospho-N-acetylmuramoyl-pentapeptide-transferase activity Ref.6 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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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

HAMAP MF_00038

Topological domain

46 – 76

Cytoplasmic Ref.7

Transmembrane

77 – 90

HAMAP MF_00038

Topological domain

91 – 96

Periplasmic Ref.7

Transmembrane

97 – 113

HAMAP MF_00038

Topological domain

114 – 133

Cytoplasmic Ref.7

Transmembrane

134 – 156

HAMAP MF_00038

Topological domain

157 – 173

Periplasmic Ref.7

Transmembrane

174 – 188

HAMAP MF_00038

Topological domain

189 – 199

Cytoplasmic Ref.7

Transmembrane

200 – 220

HAMAP MF_00038

Topological domain

221 – 238

Periplasmic Ref.7

Transmembrane

239 – 251

HAMAP MF_00038

Topological domain

252 – 270

Cytoplasmic Ref.7

Transmembrane

271 – 284

HAMAP MF_00038

Topological domain

285 – 287

Periplasmic Ref.7

Transmembrane

288 – 299

HAMAP MF_00038

Topological domain

300 – 341

Cytoplasmic Ref.7

Transmembrane

342 – 357

HAMAP MF_00038

Topological domain

358 – 360

Periplasmic Ref.7

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A6W3-1 [UniParc].

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

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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.

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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	AP_000750.1. NP_414629.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P0A6W3.
Genome annotation databases
GeneID	944814.
GenomeReviews	Gene locus JW0085 in contig AP009048_GR. Gene locus b0087 in contig U00096_GR.
KEGG	ecj:JW0085. eco:b0087.
Organism-specific databases
EchoBASE	EB0599.
EcoGene	EG10604. mraY.
CMR	Search...
Phylogenomic databases
eggNOG	COG0472.
HOGENOM	HBG708263.
OMA	HHHFEQK.
Enzyme and pathway databases
BioCyc	EcoCyc:PHOSNACMURPENTATRANS-MONOMER. ECOL168927:B0087-MONOMER. MetaCyc:PHOSNACMURPENTATRANS-MONOMER.
Gene expression databases
Genevestigator	P0A6W3.
Family and domain databases
HAMAP	MF_00038. MraY. [Tree]
InterPro	IPR000715. Glycosyl_transferase_4. IPR018481. Glycosyl_Trfase_4_cons-reg. IPR003524. PNAcMuramoyl-5peptid_Trfase. IPR018480. PNAcMuramoyl-5peptid_Trfase_CS. [Graphical view]
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...

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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:	February 9, 2010
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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 and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents