Phospho-N-acetylmuramoyl-pentapeptide-transferase

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Q7VUQ0 (MRAY_BORPE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phospho-N-acetylmuramoyl-pentapeptide-transferase
EC=2.7.8.13

Alternative name(s):
UDP-MurNAc-pentapeptide phosphotransferase

Gene names

Name:	mraY
Ordered Locus Names:	BP3026

Organism

Bordetella pertussis

Taxonomic identifier

520 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan By similarity. HAMAP MF_00038
Catalytic activity	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. HAMAP MF_00038
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00038
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity HAMAP MF_00038.
Sequence similarities	Belongs to the glycosyltransferase 4 family. MraY subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity Inferred from electronic annotation. Source: EC phospho-N-acetylmuramoyl-pentapeptide-transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 377

377

Phospho-N-acetylmuramoyl-pentapeptide-transferase HAMAP MF_00038

PRO_0000108793

Regions

Transmembrane

9 – 29

Helical; Potential

Transmembrane

59 – 79

Helical; Potential

Transmembrane

85 – 105

Helical; Potential

Transmembrane

122 – 142

Helical; Potential

Transmembrane

155 – 175

Helical; Potential

Transmembrane

178 – 198

Helical; Potential

Transmembrane

210 – 230

Helical; Potential

Transmembrane

247 – 267

Helical; Potential

Transmembrane

274 – 294

Helical; Potential

Transmembrane

299 – 319

Helical; Potential

Transmembrane

354 – 374

Helical; Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q7VUQ0 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 3440248BAD69BF1C
Show »

FASTA

377

41,315

        10         20         30         40         50         60 
MRAIGVFEYI TLRAVLACAT ALLIGLVAGP RVIRRLTEMK IGQAVRAYGP ESHLVKTGTP 

        70         80         90        100        110        120 
TMGGALILIA IAISTLLWAD WTNRFVWVVL LVTFGFGWIG WMDDYRKVVY RDPEGMPARQ 

       130        140        150        160        170        180 
KFFWQATIGL VAAVYLAFAV SAPANTELWP LFKAWVGSGF TMPLPTRADL IVPFFKSVSY 

       190        200        210        220        230        240 
PLGVLGFVAL TWAVIVGTSN AVNLTDGLDG LAIMPTVMVG SALGIFAYVV GRVDYSKYLL 

       250        260        270        280        290        300 
FPYIPGAAEL MVLCAAIGGA GLAFLWFNAY PAQVFMGDVG ALALGGALGT IAVIVRQEIV 

       310        320        330        340        350        360 
LFIMGGVFVV ETLSVMVQVT WFKYTKRKYG QGRRIFRMAP LHHHFEVGGW KETQVVVRFW 

       370 
IITMMLVLVG LSTLKLR

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References

[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.

Maskell D.J.
Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640420 Genomic DNA. Translation: CAE43297.1.
RefSeq	NP_881601.1. NC_002929.2.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2665874.
GenomeReviews	Gene locus BP3026 in contig BX470248_GR.
KEGG	bpe:BP3026.
PATRIC	21159590. VBIBorPer7866_3272.
Phylogenomic databases
HOGENOM	HBG708263.
OMA	RFWIISM.
PhylomeDB	Q7VUQ0.
ProtClustDB	PRK00108.
Enzyme and pathway databases
BioCyc	BPER257313:BP3026-MONOMER.
Family and domain databases
HAMAP	MF_00038. MraY. [Tree]
InterPro	IPR000715. Glycosyl_transferase_4. IPR003524. PNAcMuramoyl-5peptid_Trfase. IPR018480. PNAcMuramoyl-5peptid_Trfase_CS. [Graphical view]
KO	K01000.
PANTHER	PTHR22926. Glyco_trans_4. 1 hit. PTHR22926:SF3. PNAcPpept_trans. 1 hit.
Pfam	PF00953. Glycos_transf_4. 1 hit. [Graphical view]
TIGRFAMs	TIGR00445. MraY. 1 hit.
PROSITE	PS01347. MRAY_1. 1 hit. PS01348. MRAY_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MRAY_BORPE

Accession

Primary (citable) accession number: Q7VUQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents