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Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Legionella pneumophila (strain Paris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan.UniRule annotation

Catalytic activityi

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.UniRule annotation

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciLPNE297246:GCO9-3399-MONOMER.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospho-N-acetylmuramoyl-pentapeptide-transferaseUniRule annotation (EC:2.7.8.13UniRule annotation)
Alternative name(s):
UDP-MurNAc-pentapeptide phosphotransferaseUniRule annotation
Gene namesi
Name:mraYUniRule annotation
Ordered Locus Names:lpp2670
OrganismiLegionella pneumophila (strain Paris)
Taxonomic identifieri297246 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Organism-specific databases

LegioListilpp2670.

Subcellular locationi

  • Cell inner membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei27 – 4721HelicalUniRule annotationAdd
BLAST
Transmembranei70 – 9021HelicalUniRule annotationAdd
BLAST
Transmembranei97 – 11721HelicalUniRule annotationAdd
BLAST
Transmembranei134 – 15421HelicalUniRule annotationAdd
BLAST
Transmembranei167 – 18721HelicalUniRule annotationAdd
BLAST
Transmembranei199 – 21921HelicalUniRule annotationAdd
BLAST
Transmembranei236 – 25621HelicalUniRule annotationAdd
BLAST
Transmembranei263 – 28321HelicalUniRule annotationAdd
BLAST
Transmembranei288 – 30821HelicalUniRule annotationAdd
BLAST
Transmembranei338 – 35821HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 361361Phospho-N-acetylmuramoyl-pentapeptide-transferasePRO_0000108842Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi297246.lpp2670.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 4 family. MraY subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CPY. Bacteria.
COG0472. LUCA.
HOGENOMiHOG000275124.
KOiK01000.
OMAiHQNKKDT.
OrthoDBiEOG69GZPZ.

Family and domain databases

HAMAPiMF_00038. MraY.
InterProiIPR000715. Glycosyl_transferase_4.
IPR003524. PNAcMuramoyl-5peptid_Trfase.
IPR018480. PNAcMuramoyl-5peptid_Trfase_CS.
[Graphical view]
PANTHERiPTHR22926. PTHR22926. 1 hit.
PfamiPF00953. Glycos_transf_4. 1 hit.
PF10555. MraY_sig1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00445. mraY. 1 hit.
PROSITEiPS01347. MRAY_1. 1 hit.
PS01348. MRAY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5X1S3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLYWLTQLLQ GQYHAFRVFQ YLTFRSILAS LTALIVGLLC GPLMIRWLRG
60 70 80 90 100
LQIGQMVRSD GPQTHLSKAG TPTMGGVLIL LAITVSCLLW CDLRQTSLWL
110 120 130 140 150
VLLVTLANGL VGWVDDYRKL VLKNSKGLPG RWKYFWQSVI ALVAVSYLYW
160 170 180 190 200
NASLPVHTQL TVPFFKTVTW DLGVFFPVLA YFVIVGSSNA VNLTDGLDGL
210 220 230 240 250
AIMPIVMVAG ALGVFAYASS NAVYSNYLGI PYVPNTGELT IFCSSIVGAG
260 270 280 290 300
LGFLWYNSYP AQVFMGDVGS LALGAALGIV AIVVRQELVL LIMGGLFVIE
310 320 330 340 350
TLSVILQVGY FKYSGGKRLF RMAPLHHHFE LKGWSEPKVI VRFWIITVVF
360
VLCGLATLKL R
Length:361
Mass (Da):39,869
Last modified:November 23, 2004 - v1
Checksum:iC98CC373AA469E83
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628336 Genomic DNA. Translation: CAH13823.1.
RefSeqiWP_011947536.1. NC_006368.1.

Genome annotation databases

EnsemblBacteriaiCAH13823; CAH13823; lpp2670.
KEGGilpp:lpp2670.
PATRICi22325993. VBILegPne27771_3033.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628336 Genomic DNA. Translation: CAH13823.1.
RefSeqiWP_011947536.1. NC_006368.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi297246.lpp2670.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH13823; CAH13823; lpp2670.
KEGGilpp:lpp2670.
PATRICi22325993. VBILegPne27771_3033.

Organism-specific databases

LegioListilpp2670.

Phylogenomic databases

eggNOGiENOG4105CPY. Bacteria.
COG0472. LUCA.
HOGENOMiHOG000275124.
KOiK01000.
OMAiHQNKKDT.
OrthoDBiEOG69GZPZ.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciLPNE297246:GCO9-3399-MONOMER.

Family and domain databases

HAMAPiMF_00038. MraY.
InterProiIPR000715. Glycosyl_transferase_4.
IPR003524. PNAcMuramoyl-5peptid_Trfase.
IPR018480. PNAcMuramoyl-5peptid_Trfase_CS.
[Graphical view]
PANTHERiPTHR22926. PTHR22926. 1 hit.
PfamiPF00953. Glycos_transf_4. 1 hit.
PF10555. MraY_sig1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00445. mraY. 1 hit.
PROSITEiPS01347. MRAY_1. 1 hit.
PS01348. MRAY_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
    Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
    Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Paris.

Entry informationi

Entry nameiMRAY_LEGPA
AccessioniPrimary (citable) accession number: Q5X1S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 23, 2004
Last modified: November 11, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.