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Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Francisella tularensis subsp. tularensis (strain WY96-3418)
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

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:FTW_1620
OrganismiFrancisella tularensis subsp. tularensis (strain WY96-3418)
Taxonomic identifieri418136 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei22 – 42HelicalUniRule annotationAdd BLAST21
Transmembranei74 – 94HelicalUniRule annotationAdd BLAST21
Transmembranei95 – 115HelicalUniRule annotationAdd BLAST21
Transmembranei133 – 153HelicalUniRule annotationAdd BLAST21
Transmembranei168 – 188HelicalUniRule annotationAdd BLAST21
Transmembranei201 – 221HelicalUniRule annotationAdd BLAST21
Transmembranei240 – 260HelicalUniRule annotationAdd BLAST21
Transmembranei267 – 287HelicalUniRule annotationAdd BLAST21
Transmembranei292 – 312HelicalUniRule annotationAdd BLAST21
Transmembranei342 – 362HelicalUniRule annotationAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000029811 – 365Phospho-N-acetylmuramoyl-pentapeptide-transferaseAdd BLAST365

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000275122.
KOiK01000.
OMAiHQNKKDT.

Family and domain databases

CDDicd06852. GT_MraY. 1 hit.
HAMAPiMF_00038. MraY. 1 hit.
InterProiIPR000715. Glycosyl_transferase_4.
IPR003524. PNAcMuramoyl-5peptid_Trfase.
IPR018480. PNAcMuramoyl-5peptid_Trfase_CS.
[Graphical view]
PANTHERiPTHR22926. PTHR22926. 2 hits.
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.

A4IZH0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIYLFEWLS HYFKGLEVFS NYISVRIIMI SITSLLITLA LGRPMISWLQ
60 70 80 90 100
KMQIGQIVRD DGPQSHFSKR NTPTMGGVLI LSSVIISCLL WGDLTSIYLW
110 120 130 140 150
ILILVVIFFG AIGFFDDYLK LVLKHPKGLR AKYKFALQSI FSIVLAIVLF
160 170 180 190 200
YLLSKNGQMS LSIPFSKSLY IPMGIVIFVV LAFFIINGSS NAVNLTDGLD
210 220 230 240 250
GLAIVPVVLV AAGLGIYAYI ETNSTLANYL LFNYLGNPGL AEVAVFCAAV
260 270 280 290 300
CGSGLAFLWF NSHPAEVFMG DVGSLTLGAV LGVIAVMVRQ ELIFFIMGLL
310 320 330 340 350
FVVEALSVML QVGSYKLRNG KRIFRMAPIH HHFELKGWPE TKVVIRFWII
360
SLILFLIGLA AIKVR
Length:365
Mass (Da):40,547
Last modified:May 1, 2007 - v1
Checksum:iF6A01C929D1E06B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000608 Genomic DNA. Translation: ABO47320.1.
RefSeqiWP_003026957.1. NC_009257.1.

Genome annotation databases

EnsemblBacteriaiABO47320; ABO47320; FTW_1620.
KEGGiftw:FTW_1620.
PATRICi17970719. VBIFraTul58433_1664.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000608 Genomic DNA. Translation: ABO47320.1.
RefSeqiWP_003026957.1. NC_009257.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABO47320; ABO47320; FTW_1620.
KEGGiftw:FTW_1620.
PATRICi17970719. VBIFraTul58433_1664.

Phylogenomic databases

HOGENOMiHOG000275122.
KOiK01000.
OMAiHQNKKDT.

Enzyme and pathway databases

UniPathwayiUPA00219.

Family and domain databases

CDDicd06852. GT_MraY. 1 hit.
HAMAPiMF_00038. MraY. 1 hit.
InterProiIPR000715. Glycosyl_transferase_4.
IPR003524. PNAcMuramoyl-5peptid_Trfase.
IPR018480. PNAcMuramoyl-5peptid_Trfase_CS.
[Graphical view]
PANTHERiPTHR22926. PTHR22926. 2 hits.
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...

Entry informationi

Entry nameiMRAY_FRATW
AccessioniPrimary (citable) accession number: A4IZH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 2007
Last modified: November 2, 2016
This is version 69 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.