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Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Pelobacter propionicus (strain DSM 2379)
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

BioCyciPPRO338966:GHL0-3349-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:Ppro_3292
OrganismiPelobacter propionicus (strain DSM 2379)
Taxonomic identifieri338966 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesDesulfuromonadaceaePelobacter
Proteomesi
  • UP000006732 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
Transmembranei97 – 11721HelicalUniRule annotationAdd
BLAST
Transmembranei134 – 15421HelicalUniRule annotationAdd
BLAST
Transmembranei170 – 19021HelicalUniRule annotationAdd
BLAST
Transmembranei197 – 21721HelicalUniRule annotationAdd
BLAST
Transmembranei233 – 25321HelicalUniRule annotationAdd
BLAST
Transmembranei261 – 28121HelicalUniRule annotationAdd
BLAST
Transmembranei286 – 30621HelicalUniRule annotationAdd
BLAST
Transmembranei335 – 35521HelicalUniRule 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 – 358358Phospho-N-acetylmuramoyl-pentapeptide-transferasePRO_1000003027Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi338966.Ppro_3292.

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.
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.

A1AU64-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLYHLLYPLA GDVKLFNIFK YLTFRTIYAM ITALLVCFVL GPWVIRVLEG
60 70 80 90 100
LQARQVIRTD GPESHLQKQG TPTMGGVMIL AAIVIPTLLW ADLSNQYIWT
110 120 130 140 150
VLFITIGYGL IGFVDDYKKV VEKNPKGLSP RQKMFWQVLL AGAVGTFLFL
160 170 180 190 200
KPGFNAQLFV PFFKNFHPDL WFWYIPFVTL VIVGASNAVN LTDGLDGLAI
210 220 230 240 250
GPVAINAATY MLFSYVAGHA TLSAYLQVPR VAGAGELAVL CGAMVGAGLG
260 270 280 290 300
FLWYNSYPAE VFMGDVGSLS LGGTLGAIAV ITKQEILLVI VGGIFVIEAL
310 320 330 340 350
SVIFQVGSYK YRGKRIFRMA PIHHHFELKG VAEPKIIVRF WIITIILALV

AISTLKMR
Length:358
Mass (Da):39,454
Last modified:January 23, 2007 - v1
Checksum:iA07215C61530354B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000482 Genomic DNA. Translation: ABL00885.1.
RefSeqiWP_011737102.1. NC_008609.1.

Genome annotation databases

EnsemblBacteriaiABL00885; ABL00885; Ppro_3292.
KEGGippd:Ppro_3292.
PATRICi22899723. VBIPelPro64470_3448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000482 Genomic DNA. Translation: ABL00885.1.
RefSeqiWP_011737102.1. NC_008609.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi338966.Ppro_3292.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABL00885; ABL00885; Ppro_3292.
KEGGippd:Ppro_3292.
PATRICi22899723. VBIPelPro64470_3448.

Phylogenomic databases

eggNOGiENOG4105CPY. Bacteria.
COG0472. LUCA.
HOGENOMiHOG000275122.
KOiK01000.
OMAiHQNKKDT.
OrthoDBiEOG69GZPZ.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciPPRO338966:GHL0-3349-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 chromosome of Pelobacter propionicus DSM 2379."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.
    , Land M., Hauser L., Kyrpides N., Kim E., Lovley D., Richardson P.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2379.

Entry informationi

Entry nameiMRAY_PELPD
AccessioniPrimary (citable) accession number: A1AU64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: June 8, 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

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.