Phospho-N-acetylmuramoyl-pentapeptide-transferase - Escherichia coli O9:H4 (strain HS)

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A7ZW39 (MRAY_ECOHS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. 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:	EcHS_A0093

Organism

Escherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]

Taxonomic identifier

331112 [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-Rule 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-Rule MF_00038
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00038
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule 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 peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP 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: HAMAP
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-Rule MF_00038

PRO_1000057276

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

A7ZW39 [UniParc].

Last modified October 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 pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000802 Genomic DNA. Translation: ABV04493.1.
RefSeq	YP_001456876.1. NC_009800.1.
3D structure databases
ProteinModelPortal	A7ZW39.
ModBase	Search...
Protein-protein interaction databases
IntAct	A7ZW39. 1 interaction.
STRING	331112.EcHS_A0093.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABV04493; ABV04493; EcHS_A0093.
GeneID	5594239.
KEGG	ecx:EcHS_A0093.
PATRIC	18310179. VBIEscCol77814_0093.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0472.
HOGENOM	HOG000275122.
KO	K01000.
OMA	EYLTQFY.
ProtClustDB	PRK00108.
Enzyme and pathway databases
BioCyc	ECOL331112:GHHI-250-MONOMER.
UniPathway	UPA00219.
Family and domain databases
HAMAP	MF_00038. MraY.
InterPro	IPR000715. Glycosyl_transferase_4. IPR003524. PNAcMuramoyl-5peptid_Trfase. IPR018480. PNAcMuramoyl-5peptid_Trfase_CS. [Graphical view]
PANTHER	PTHR22926. PTHR22926. 1 hit. PTHR22926:SF3. PTHR22926:SF3. 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...
Other
BindingDB	A7ZW39.

Entry information

Entry name

MRAY_ECOHS

Accession

Primary (citable) accession number: A7ZW39

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	May 1, 2013
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

Other

Entry information

Relevant documents