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Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Staphylococcus aureus (strain N315)
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.By similarity

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.

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.
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

Keywordsi

Molecular functionTransferase
Biological processCell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospho-N-acetylmuramoyl-pentapeptide-transferase (EC:2.7.8.13)
Alternative name(s):
UDP-MurNAc-pentapeptide phosphotransferase
Gene namesi
Name:mraY
Ordered Locus Names:SA1025
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000751 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei1 – 21HelicalBy similarityAdd BLAST21
Topological domaini22 – 52CytoplasmicSequence analysisAdd BLAST31
Transmembranei53 – 69HelicalBy similarityAdd BLAST17
Topological domaini70 – 75ExtracellularSequence analysis6
Transmembranei76 – 91HelicalBy similarityAdd BLAST16
Topological domaini92 – 111CytoplasmicSequence analysisAdd BLAST20
Transmembranei112 – 133HelicalBy similarityAdd BLAST22
Topological domaini134 – 150ExtracellularSequence analysisAdd BLAST17
Transmembranei151 – 165HelicalBy similarityAdd BLAST15
Topological domaini166 – 176CytoplasmicSequence analysisAdd BLAST11
Transmembranei177 – 197HelicalBy similarityAdd BLAST21
Topological domaini198 – 202ExtracellularSequence analysis5
Transmembranei203 – 216HelicalBy similarityAdd BLAST14
Topological domaini217 – 232CytoplasmicSequence analysisAdd BLAST16
Transmembranei233 – 246HelicalBy similarityAdd BLAST14
Topological domaini247 – 249ExtracellularSequence analysis3
Transmembranei250 – 268HelicalBy similarityAdd BLAST19
Topological domaini269 – 300CytoplasmicSequence analysisAdd BLAST32
Transmembranei301 – 320HelicalBy similarityAdd BLAST20
Topological domaini321ExtracellularSequence analysis1

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001088921 – 321Phospho-N-acetylmuramoyl-pentapeptide-transferaseAdd BLAST321

Structurei

3D structure databases

ProteinModelPortaliP68783.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000275124.
KOiK01000.
OMAiLMSPLHH.

Family and domain databases

CDDicd06852. GT_MraY. 1 hit.
HAMAPiMF_00038. MraY. 1 hit.
InterProiView protein in InterPro
IPR000715. Glycosyl_transferase_4.
IPR003524. PNAcMuramoyl-5peptid_Trfase.
IPR018480. PNAcMuramoyl-5peptid_Trfase_CS.
PANTHERiPTHR22926. PTHR22926. 1 hit.
PfamiView protein in Pfam
PF00953. Glycos_transf_4. 1 hit.
TIGRFAMsiTIGR00445. mraY. 1 hit.
PROSITEiView protein in PROSITE
PS01347. MRAY_1. 1 hit.
PS01348. MRAY_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P68783-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIFVYALLAL VITFVLVPVL IPTLKRMKFG QSIREEGPQS HMKKTGTPTM
60 70 80 90 100
GGLTFLLSIV ITSLVAIIFV DQANPIILLL FVTIGFGLIG FIDDYIIVVK
110 120 130 140 150
KNNQGLTSKQ KFLAQIGIAI IFFVLSNVFH LVNFSTSIHI PFTNVAIPLS
160 170 180 190 200
FAYVIFIVFW QVGFSNAVNL TDGLDGLATG LSIIGFTMYA IMSFVLGETA
210 220 230 240 250
IGIFCIIMLF ALLGFLPYNI NPAKVFMGDT GSLALGGIFA TISIMLNQEL
260 270 280 290 300
SLIFIGLVFV IETLSVMLQV ASFKLTGKRI FKMSPIHHHF ELIGWSEWKV
310 320
VTVFWAVGLI SGLIGLWIGV H
Length:321
Mass (Da):35,232
Last modified:December 21, 2004 - v1
Checksum:i0A2F82D042255848
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB42277.1.
PIRiA89890.
RefSeqiWP_000578458.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB42277; BAB42277; BAB42277.
KEGGisau:SA1025.

Similar proteinsi

Entry informationi

Entry nameiMRAY_STAAN
AccessioniPrimary (citable) accession number: P68783
Secondary accession number(s): O07322, O24815
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 21, 2004
Last modified: June 7, 2017
This is version 92 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

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