Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Salmonella typhi
Status
Reviewed-Annotation score: -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:STY0145, t0129
OrganismiSalmonella typhi
Taxonomic identifieri90370 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000002670 Componenti: Chromosome
  • UP000000541 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 25PeriplasmicSequence analysisAdd BLAST25
Transmembranei26 – 46HelicalSequence analysisAdd BLAST21
Topological domaini47 – 71CytoplasmicSequence analysisAdd BLAST25
Transmembranei72 – 92HelicalSequence analysisAdd BLAST21
Topological domaini93PeriplasmicSequence analysis1
Transmembranei94 – 114HelicalSequence analysisAdd BLAST21
Topological domaini115 – 131CytoplasmicSequence analysisAdd BLAST17
Transmembranei132 – 152HelicalSequence analysisAdd BLAST21
Topological domaini153 – 167PeriplasmicSequence analysisAdd BLAST15
Transmembranei168 – 188HelicalSequence analysisAdd BLAST21
Topological domaini189 – 198CytoplasmicSequence analysis10
Transmembranei199 – 219HelicalSequence analysisAdd BLAST21
Topological domaini220 – 235PeriplasmicSequence analysisAdd BLAST16
Transmembranei236 – 256HelicalSequence analysisAdd BLAST21
Topological domaini257 – 262CytoplasmicSequence analysis6
Transmembranei263 – 283HelicalSequence analysisAdd BLAST21
Topological domaini284 – 287PeriplasmicSequence analysis4
Transmembranei288 – 308HelicalSequence analysisAdd BLAST21
Topological domaini309 – 337CytoplasmicSequence analysisAdd BLAST29
Transmembranei338 – 358HelicalSequence analysisAdd BLAST21
Topological domaini359 – 360PeriplasmicSequence analysis2

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001088841 – 360Phospho-N-acetylmuramoyl-pentapeptide-transferaseAdd BLAST360

Interactioni

Protein-protein interaction databases

STRINGi220341.STY0145

Structurei

3D structure databases

SMRiQ8Z9H1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CPY Bacteria
COG0472 LUCA
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.

Q8Z9H1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVWLAEHLV KYYSGFNVFS YLTFRAIVSL LTALFISLWM GPRMIARLQK
60 70 80 90 100
LSFGQVVRND GPESHFSKRG TPTMGGIMIL TAIVISVLLW AYPSNPYVWC
110 120 130 140 150
VLVVLIGYGI IGFVDDYRKV VRKDTKGLIA RWKYFWMSVI ALGVAFALYL
160 170 180 190 200
VGKDTPATQL VVPFFKDVMP QLGLFYILLS YFVIVGTGNA VNLTDGLDGL
210 220 230 240 250
AIMPTVFVAA GFALVAWATG NMNFANYLHI 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):40,007
Last modified:March 1, 2002 - v1
Checksum:i74AC3E04ABCCFA72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL513382 Genomic DNA Translation: CAD01282.1
AE014613 Genomic DNA Translation: AAO67861.1
RefSeqiNP_454737.1, NC_003198.1
WP_000964138.1, NZ_QAVU01000006.1

Genome annotation databases

EnsemblBacteriaiAAO67861; AAO67861; t0129
CAD01282; CAD01282; CAD01282
GeneIDi1246640
KEGGistt:t0129
sty:STY0145
PATRICifig|220341.7.peg.145

Entry informationi

Entry nameiMRAY_SALTI
AccessioniPrimary (citable) accession number: Q8Z9H1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: March 1, 2002
Last modified: July 18, 2018
This is version 111 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health