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Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Shigella flexneri
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:SF0084, S0086
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

Subcellular locationi

P0A6W4:

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_00001088881 – 360Phospho-N-acetylmuramoyl-pentapeptide-transferaseAdd BLAST360

Proteomic databases

PaxDbiP0A6W4.

Structurei

3D structure databases

ProteinModelPortaliP0A6W4.
SMRiP0A6W4.
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.

P0A6W4-1 [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 15, 2005 - v1
Checksum:iF3550AFA3CD636AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN41749.1.
AE014073 Genomic DNA. Translation: AAP15630.1.
RefSeqiNP_706042.1. NC_004337.2.
WP_000964131.1. NZ_NGWF01000027.1.

Genome annotation databases

EnsemblBacteriaiAAN41749; AAN41749; SF0084.
AAP15630; AAP15630; S0086.
GeneIDi1024554.
KEGGisfl:SF0084.
sfx:S0086.
PATRICifig|198214.7.peg.99.

Similar proteinsi

Entry informationi

Entry nameiMRAY_SHIFL
AccessioniPrimary (citable) accession number: P0A6W4
Secondary accession number(s): P15876
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: October 25, 2017
This is version 97 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