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Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Escherichia coli O45:K1 (strain S88 / ExPEC)
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.

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:ECS88_0090
OrganismiEscherichia coli O45:K1 (strain S88 / ExPEC)
Taxonomic identifieri585035 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000747 Componenti: Chromosome

Subcellular locationi

  • Cell inner membrane ; Multi-pass membrane protein

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 25PeriplasmicAdd BLAST25
Transmembranei26 – 46HelicalAdd BLAST21
Topological domaini47 – 71CytoplasmicAdd BLAST25
Transmembranei72 – 92HelicalAdd BLAST21
Topological domaini93Periplasmic1
Transmembranei94 – 114HelicalAdd BLAST21
Topological domaini115 – 131CytoplasmicAdd BLAST17
Transmembranei132 – 152HelicalAdd BLAST21
Topological domaini153 – 167PeriplasmicAdd BLAST15
Transmembranei168 – 188HelicalAdd BLAST21
Topological domaini189 – 198Cytoplasmic10
Transmembranei199 – 219HelicalAdd BLAST21
Topological domaini220 – 235PeriplasmicAdd BLAST16
Transmembranei236 – 256HelicalAdd BLAST21
Topological domaini257 – 262Cytoplasmic6
Transmembranei263 – 283HelicalAdd BLAST21
Topological domaini284 – 287Periplasmic4
Transmembranei288 – 308HelicalAdd BLAST21
Topological domaini309 – 337CytoplasmicAdd BLAST29
Transmembranei338 – 358HelicalAdd BLAST21
Topological domaini359 – 360Periplasmic2

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001165121 – 360Phospho-N-acetylmuramoyl-pentapeptide-transferaseAdd BLAST360

Structurei

3D structure databases

ProteinModelPortaliB7MAL0.
SMRiB7MAL0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 4 family. MraY subfamily.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000275122.
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.
PF10555. MraY_sig1. 1 hit.
TIGRFAMsiTIGR00445. mraY. 1 hit.
PROSITEiView protein in PROSITE
PS01347. MRAY_1. 1 hit.
PS01348. MRAY_2. 1 hit.

Sequencei

Sequence statusi: Complete.

B7MAL0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVWLAEHLV KYYSGFNVFS YLTFRAIVSL LTALFISLWM GPRMIAHLQK
60 70 80 90 100
LSFGQVVRND GPESHFSKRG TPTMGGIMIL TAIVISVLLW AYPSNPYVWC
110 120 130 140 150
VLVVLVGYGV IGFVDDYRKV VRKDTKGLIA RWKYFWMSVI ALGVAFALYL
160 170 180 190 200
AGKDTPATQL VVPFFKDVMP QLGLFYILLA YFVIVGTGNA VNLTDGLDGL
210 220 230 240 250
AIMPTVFVAG GFALVAWATG NMNFASYLHI PYLRHAGELV IVCTAIVGAG
260 270 280 290 300
LGFLWFNTYP AQVFMGDVGS LALGGALGII AVLLRQEFLL VIMGGVFVVE
310 320 330 340 350
TLSVILQVGS FKLRGQRIFR MAPIHHHYEL KGWPEPRVIV RFWIISLMLV
360
LIGLATLKVR
Length:360
Mass (Da):39,875
Last modified:March 24, 2009 - v1
Checksum:iF3550AFA3CD636AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928161 Genomic DNA. Translation: CAR01456.1.
RefSeqiWP_000964131.1. NC_011742.1.

Genome annotation databases

EnsemblBacteriaiCAR01456; CAR01456; ECS88_0090.
KEGGiecz:ECS88_0090.

Similar proteinsi

Entry informationi

Entry nameiMRAY_ECO45
AccessioniPrimary (citable) accession number: B7MAL0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: March 24, 2009
Last modified: November 22, 2017
This is version 59 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