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Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
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

BioCyciRRUB269796:GCN1-974-MONOMER.
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:Rru_A0953
OrganismiRhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Taxonomic identifieri269796 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum
Proteomesi
  • UP000001929 Componenti: Chromosome

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei27 – 4721HelicalUniRule annotationAdd
BLAST
Transmembranei73 – 9321HelicalUniRule annotationAdd
BLAST
Transmembranei98 – 11821HelicalUniRule annotationAdd
BLAST
Transmembranei134 – 15421HelicalUniRule annotationAdd
BLAST
Transmembranei168 – 18821HelicalUniRule annotationAdd
BLAST
Transmembranei199 – 21921HelicalUniRule annotationAdd
BLAST
Transmembranei239 – 25921HelicalUniRule annotationAdd
BLAST
Transmembranei263 – 28321HelicalUniRule annotationAdd
BLAST
Transmembranei288 – 30821HelicalUniRule annotationAdd
BLAST
Transmembranei337 – 35721HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 360360Phospho-N-acetylmuramoyl-pentapeptide-transferasePRO_0000235476Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi269796.Rru_A0953.

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.
HOGENOMiHOG000275124.
KOiK01000.
OMAiHQNKKDT.
OrthoDBiEOG69GZPZ.

Family and domain databases

HAMAPiMF_00038. MraY.
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.

Q2RVU1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLYFLSELTA QVSALNVFRY LTFRTGGAVM TAMLVAFVFG PGIIEWLKRK
60 70 80 90 100
QGEGQPIRSD GPESHLTKKG TPTMGGIMIL LGVGVATLLW ADLSKGYVWA
110 120 130 140 150
VLLLTLGYGA IGFADDYLKL TKRNTKGLSG RLKLVAQVGM AVIAGLWIML
160 170 180 190 200
LGQGDQASSL ALPFFKDLTF NLGWFYLPFA AFVMVGASNA VNLTDGLDGL
210 220 230 240 250
AIVPVMIAAG VFMLIAYLVG NIIFSNYLQI QHVPGTGELA VFCGAIVGAA
260 270 280 290 300
VGFLWFNAPP AMVFMGDTGS LALGGALGAV SVVTKHEIVL AIVGGLFVLE
310 320 330 340 350
TVSVIVQVAS FKLTGKRVFR MAPLHHHFEK KGWAEPTVVI RFWIIAMILA
360
IVGLSTLKLR
Length:360
Mass (Da):38,513
Last modified:January 24, 2006 - v1
Checksum:i2ACDA225D9519064
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000230 Genomic DNA. Translation: ABC21754.1.
RefSeqiWP_011388708.1. NC_007643.1.
YP_426041.1. NC_007643.1.

Genome annotation databases

EnsemblBacteriaiABC21754; ABC21754; Rru_A0953.
GeneIDi3833626.
KEGGirru:Rru_A0953.
PATRICi23325500. VBIRhoRub82919_1009.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000230 Genomic DNA. Translation: ABC21754.1.
RefSeqiWP_011388708.1. NC_007643.1.
YP_426041.1. NC_007643.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269796.Rru_A0953.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC21754; ABC21754; Rru_A0953.
GeneIDi3833626.
KEGGirru:Rru_A0953.
PATRICi23325500. VBIRhoRub82919_1009.

Phylogenomic databases

eggNOGiENOG4105CPY. Bacteria.
COG0472. LUCA.
HOGENOMiHOG000275124.
KOiK01000.
OMAiHQNKKDT.
OrthoDBiEOG69GZPZ.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciRRUB269796:GCN1-974-MONOMER.

Family and domain databases

HAMAPiMF_00038. MraY.
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...

Publicationsi

  1. "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.
    , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C.
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1.

Entry informationi

Entry nameiMRAY_RHORT
AccessioniPrimary (citable) accession number: Q2RVU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: January 24, 2006
Last modified: November 11, 2015
This is version 75 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

Complete proteome, Reference proteome

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.