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Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
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

Pathway:ipeptidoglycan 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

BioCyciBBRO257310:BB4201-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:BB4201
OrganismiBordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
Taxonomic identifieri257310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000001027 Componenti: Chromosome

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei9 – 2921HelicalUniRule annotationAdd
BLAST
Transmembranei59 – 7921HelicalUniRule annotationAdd
BLAST
Transmembranei85 – 10521HelicalUniRule annotationAdd
BLAST
Transmembranei122 – 14221HelicalUniRule annotationAdd
BLAST
Transmembranei155 – 17521HelicalUniRule annotationAdd
BLAST
Transmembranei178 – 19821HelicalUniRule annotationAdd
BLAST
Transmembranei210 – 23021HelicalUniRule annotationAdd
BLAST
Transmembranei247 – 26721HelicalUniRule annotationAdd
BLAST
Transmembranei274 – 29421HelicalUniRule annotationAdd
BLAST
Transmembranei299 – 31921HelicalUniRule annotationAdd
BLAST
Transmembranei354 – 37421HelicalUniRule 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 – 377377Phospho-N-acetylmuramoyl-pentapeptide-transferasePRO_0000108789Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi257310.BB4201.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0472.
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.
[Graphical view]
TIGRFAMsiTIGR00445. mraY. 1 hit.
PROSITEiPS01347. MRAY_1. 1 hit.
PS01348. MRAY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7WFR9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAIGVFEYI TLRAVLACAT ALLIGLVAGP RVIRRLTEMK IGQAVRAYGP
60 70 80 90 100
ESHLVKTGTP TMGGALILIA IAISTLLWAD WTNRFVWVVL LVTFGFGWIG
110 120 130 140 150
WMDDYRKVVY RDPEGMPARQ KFFWQATIGL VAAVYLAFAV SAPANTELWP
160 170 180 190 200
LFKAWVGSGF TMPLPTRADL IVPFFKSVSY PLGVLGFVAL TWAVIVGTSN
210 220 230 240 250
AVNLTDGLDG LAIMPTVMVG SALGIFAYVV GRVDYSKYLL FPYIPGAAEL
260 270 280 290 300
MVLCAAIGGA GLAFLWFNAY PAQVFMGDVG ALALGGALGT IAVIVRQEIV
310 320 330 340 350
LFIMGGVFVV ETLSVMVQVT WFKYTKRKYG QGRRIFRMAP LHHHFEVGGW
360 370
KETQVVVRFW IITMMLVLVG LSTLKLR
Length:377
Mass (Da):41,315
Last modified:October 1, 2003 - v1
Checksum:i3440248BAD69BF1C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640449 Genomic DNA. Translation: CAE34565.1.

Genome annotation databases

EnsemblBacteriaiCAE34565; CAE34565; BB4201.
KEGGibbr:BB4201.
PATRICi21141829. VBIBorBro124907_4267.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640449 Genomic DNA. Translation: CAE34565.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi257310.BB4201.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE34565; CAE34565; BB4201.
KEGGibbr:BB4201.
PATRICi21141829. VBIBorBro124907_4267.

Phylogenomic databases

eggNOGiCOG0472.
HOGENOMiHOG000275122.
KOiK01000.
OMAiHQNKKDT.
OrthoDBiEOG69GZPZ.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciBBRO257310:BB4201-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.
[Graphical view]
TIGRFAMsiTIGR00445. mraY. 1 hit.
PROSITEiPS01347. MRAY_1. 1 hit.
PS01348. MRAY_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
    Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
    , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
    Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-588 / NCTC 13252 / RB50.

Entry informationi

Entry nameiMRAY_BORBR
AccessioniPrimary (citable) accession number: Q7WFR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 1, 2003
Last modified: July 22, 2015
This is version 82 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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.