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
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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:aq_053
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei26 – 46HelicalUniRule annotationAdd BLAST21
Transmembranei73 – 93HelicalUniRule annotationAdd BLAST21
Transmembranei100 – 120HelicalUniRule annotationAdd BLAST21
Transmembranei143 – 163HelicalUniRule annotationAdd BLAST21
Transmembranei166 – 186HelicalUniRule annotationAdd BLAST21
Transmembranei197 – 217HelicalUniRule annotationAdd BLAST21
Transmembranei234 – 254HelicalUniRule annotationAdd BLAST21
Transmembranei261 – 281HelicalUniRule annotationAdd BLAST21
Transmembranei287 – 307HelicalUniRule annotationAdd BLAST21
Transmembranei336 – 356HelicalUniRule 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_00001087721 – 359Phospho-N-acetylmuramoyl-pentapeptide-transferaseAdd BLAST359

Interactioni

Protein-protein interaction databases

DIPiDIP-61734N.
STRINGi224324.aq_053.

Structurei

Secondary structure

1359
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 56Combined sources36
Beta strandi71 – 73Combined sources3
Helixi78 – 92Combined sources15
Turni95 – 97Combined sources3
Helixi99 – 124Combined sources26
Helixi130 – 149Combined sources20
Beta strandi157 – 159Combined sources3
Beta strandi167 – 169Combined sources3
Helixi171 – 173Combined sources3
Helixi174 – 192Combined sources19
Helixi200 – 216Combined sources17
Helixi220 – 225Combined sources6
Helixi235 – 255Combined sources21
Beta strandi256 – 258Combined sources3
Helixi264 – 281Combined sources18
Helixi285 – 291Combined sources7
Helixi293 – 312Combined sources20
Beta strandi317 – 322Combined sources6
Helixi323 – 329Combined sources7
Helixi334 – 356Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4J72X-ray3.30A/B1-359[»]
5CKRX-ray2.95A1-359[»]
SMRiO66465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CPY. Bacteria.
COG0472. LUCA.
HOGENOMiHOG000275122.
InParanoidiO66465.
KOiK01000.
OMAiHQNKKDT.
OrthoDBiPOG091H00VH.

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. 1 hit.
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.

O66465-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLYQLALLLK DYWFAFNVLK YITFRSFTAV LIAFFLTLVL SPSFINRLRK
60 70 80 90 100
IQRLFGGYVR EYTPESHEVK KYTPTMGGIV ILIVVTLSTL LLMRWDIKYT
110 120 130 140 150
WVVLLSFLSF GTIGFWDDYV KLKNKKGISI KTKFLLQVLS ASLISVLIYY
160 170 180 190 200
WADIDTILYF PFFKELYVDL GVLYLPFAVF VIVGSANAVN LTDGLDGLAI
210 220 230 240 250
GPAMTTATAL GVVAYAVGHS KIAQYLNIPY VPYAGELTVF CFALVGAGLG
260 270 280 290 300
FLWFNSFPAQ MFMGDVGSLS IGASLATVAL LTKSEFIFAV AAGVFVFETI
310 320 330 340 350
SVILQIIYFR WTGGKRLFKR APFHHHLELN GLPEPKIVVR MWIISILLAI

IAISMLKLR
Length:359
Mass (Da):40,341
Last modified:August 1, 1998 - v1
Checksum:iB2D6292EA6EA16D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06418.1.
PIRiF70304.
RefSeqiNP_213025.1. NC_000918.1.
WP_010879963.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC06418; AAC06418; aq_053.
GeneIDi1192662.
KEGGiaae:aq_053.
PATRICi20957801. VBIAquAeo85532_0041.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06418.1.
PIRiF70304.
RefSeqiNP_213025.1. NC_000918.1.
WP_010879963.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4J72X-ray3.30A/B1-359[»]
5CKRX-ray2.95A1-359[»]
SMRiO66465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61734N.
STRINGi224324.aq_053.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC06418; AAC06418; aq_053.
GeneIDi1192662.
KEGGiaae:aq_053.
PATRICi20957801. VBIAquAeo85532_0041.

Phylogenomic databases

eggNOGiENOG4105CPY. Bacteria.
COG0472. LUCA.
HOGENOMiHOG000275122.
InParanoidiO66465.
KOiK01000.
OMAiHQNKKDT.
OrthoDBiPOG091H00VH.

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. 1 hit.
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_AQUAE
AccessioniPrimary (citable) accession number: O66465
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.