Phospho-N-acetylmuramoyl-pentapeptide-transferase

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A1A7D2 (MRAY_ECOK1) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 47. History...

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

Documents (2) |

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
Ordered Locus Names:	Ecok1_00780
ORF Names:	APECO1_1899

Organism

Escherichia coli O1:K1 / APEC [Complete proteome] [HAMAP]

Taxonomic identifier

405955 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	360 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan By similarity. HAMAP MF_00038
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
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00038
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity HAMAP MF_00038.
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
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-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 electronic annotation. Source: EC
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_1000002968

Regions

Topological domain

1 – 25

Periplasmic Potential

Transmembrane

26 – 46

Helical; Potential

Topological domain

47 – 71

Cytoplasmic Potential

Transmembrane

72 – 92

Helical; Potential

Topological domain

Periplasmic Potential

Transmembrane

94 – 114

Helical; Potential

Topological domain

115 – 131

Cytoplasmic Potential

Transmembrane

132 – 152

Helical; Potential

Topological domain

153 – 167

Periplasmic Potential

Transmembrane

168 – 188

Helical; Potential

Topological domain

189 – 198

Cytoplasmic Potential

Transmembrane

199 – 219

Helical; Potential

Topological domain

220 – 235

Periplasmic Potential

Transmembrane

236 – 256

Helical; Potential

Topological domain

257 – 262

Cytoplasmic Potential

Transmembrane

263 – 283

Helical; Potential

Topological domain

284 – 287

Periplasmic Potential

Transmembrane

288 – 308

Helical; Potential

Topological domain

309 – 337

Cytoplasmic Potential

Transmembrane

338 – 358

Helical; Potential

Topological domain

359 – 360

Periplasmic Potential

Sequences

Sequence

Length

Mass (Da)

Tools

A1A7D2 [UniParc].

Last modified January 23, 2007. 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

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References

[1]

"The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
J. Bacteriol. 189:3228-3236(2007) [PubMed: 17293413] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000468 Genomic DNA. Translation: ABI99571.1.
RefSeq	YP_851286.1. NC_008563.1.
3D structure databases
ProteinModelPortal	A1A7D2.
ModBase	Search...
Protein-protein interaction databases
STRING	A1A7D2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000035676; EBESCP00000034193; EBESCG00000034726.
GeneID	4493069.
GenomeReviews	Gene locus Ecok1_00780 in contig CP000468_GR.
KEGG	ecv:APECO1_1899.
PATRIC	18211565. VBIEscCol127180_0096.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0472.
GeneTree	EBGT00050000009109.
HOGENOM	HBG708263.
OMA	RFWIISM.
ProtClustDB	PRK00108.
Enzyme and pathway databases
BioCyc	ECOL405955:APECO1_1899-MONOMER.
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_ECOK1

Accession

Primary (citable) accession number: A1A7D2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 47 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

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

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents