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Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Lactobacillus reuteri MM2-3
Status
Unreviewed-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

GO - Molecular functioni

  1. phospho-N-acetylmuramoyl-pentapeptide-transferase activity Source: UniProtKB-HAMAP
  2. UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. cell wall organization Source: UniProtKB-KW
  4. peptidoglycan biosynthetic process Source: UniProtKB-HAMAP
  5. regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotationImported

Keywords - Biological processi

Cell cycle, Cell divisionUniRule annotation, Cell shape, Cell wall biogenesis/degradationUniRule annotation, Peptidoglycan synthesisUniRule annotation

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 annotationImported
ORF Names:HMPREF0535_1613Imported
OrganismiLactobacillus reuteri MM2-3Imported
Taxonomic identifieri585517 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Subcellular locationi

  1. Cell membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei37 – 5721HelicalUniRule annotationAdd
BLAST
Transmembranei61 – 8121HelicalUniRule annotationAdd
BLAST
Transmembranei98 – 11821HelicalUniRule annotationAdd
BLAST
Transmembranei120 – 14021HelicalUniRule annotationAdd
BLAST
Transmembranei153 – 17321HelicalUniRule annotationAdd
BLAST
Transmembranei176 – 19621HelicalUniRule annotationAdd
BLAST
Transmembranei205 – 22723HelicalUniRule annotationAdd
BLAST
Transmembranei231 – 25323HelicalUniRule annotationAdd
BLAST
Transmembranei282 – 30221HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membraneUniRule annotation, Membrane

Structurei

3D structure databases

ProteinModelPortaliC0Z0P8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helixUniRule annotation

Phylogenomic databases

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.

C0Z0P8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSLIKYFRA KKEGQQIRKE GPTWHAKKAG TPTMGGLLFI FSAVVTILWV
60 70 80 90 100
AAWQGLITNT LWALLFVLVV YGLIGMWDDS IKIFHHQNEG FKPWQKALCQ
110 120 130 140 150
VLAAMVFTVI YQHEGFQMGF GTTQIGWLYG LFIIFWIVGF SNAVNLTDGL
160 170 180 190 200
DGLVSGLSII SFAAYLIIAL VNLNQPGYPE IALFCLAMIG TLLGFFPYNH
210 220 230 240 250
KPAKIFMGDM GSLAIGASLA AVSLLLHHEW SLLVIGIVYV CETASVILQV
260 270 280 290 300
ASFKTTGKRI FKMTPIHHHF EMSGWSEWKI DIVFWLVGLV AAIIAVTTIL

LVG
Length:303
Mass (Da):33,569
Last modified:May 26, 2009 - v1
Checksum:i702E9CDF428CEAA3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ACLB01000090 Genomic DNA. Translation: EEI08559.1.

Genome annotation databases

EnsemblBacteriaiEEI08559; EEI08559; HMPREF0535_1613.
PATRICi37024688. VBILacReu127513_1232.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ACLB01000090 Genomic DNA. Translation: EEI08559.1.

3D structure databases

ProteinModelPortaliC0Z0P8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiEEI08559; EEI08559; HMPREF0535_1613.
PATRICi37024688. VBILacReu127513_1232.

Phylogenomic databases

OrthoDBiEOG69GZPZ.

Enzyme and pathway databases

UniPathwayiUPA00219.

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. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MM2-3Imported.

Entry informationi

Entry nameiC0Z0P8_LACRE
AccessioniPrimary (citable) accession number: C0Z0P8
Entry historyi
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: February 4, 2015
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

External Data

Dasty 3

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 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.