Phospho-N-acetylmuramoyl-pentapeptide-transferase - Borrelia burgdorferi (Lyme disease spirochete)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q44776 (MRAY_BORBU)

Last modified February 9, 2010. Version 75. History...

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

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

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:	BB_0303

Organism

Borrelia burgdorferi (Lyme disease spirochete) [Complete proteome] [HAMAP]

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Hide | Top

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

Hide | Top

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.

Hide | Top

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
Molecular function	Transferase
Technical term	Complete 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-SubCell plasma membrane Inferred from electronic annotation. Source: HAMAP
Molecular function	phospho-N-acetylmuramoyl-pentapeptide-transferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 351

351

Phospho-N-acetylmuramoyl-pentapeptide-transferase HAMAP MF_00038

PRO_0000108790

Regions

Transmembrane

17 – 37

Potential

Transmembrane

62 – 82

Potential

Transmembrane

85 – 105

Potential

Transmembrane

130 – 150

Potential

Transmembrane

158 – 178

Potential

Transmembrane

190 – 210

Potential

Transmembrane

230 – 250

Potential

Transmembrane

254 – 274

Potential

Transmembrane

279 – 299

Potential

Transmembrane

328 – 348

Potential

Experimental info

Sequence conflict

L → C in CAA65460. Ref.3

Sequence conflict

L → C in CAA65292. Ref.3

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q44776-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F6FE800C0C6151E3
Show »

FASTA

351

39,480

        10         20         30         40         50         60 
MFYLLGLRLL KYITFRMAYA TIFAFLLSLI VGPYIILKLK KLRADQILRE DGPKRHLSEK 

        70         80         90        100        110        120 
AGIPTMGGIL IFFCVFISLV FWSNILNVYF LIMVFVMLGF AFLGFIDDFL KIKKKTSDGL 

       130        140        150        160        170        180 
KARFKIYGQI IFSFFSVGIL YYFGGEHVSV IYFPFIKSFQ IDLGLFYIPF GMFILISASN 

       190        200        210        220        230        240 
SFNLTDGLDG LAIGLSIVIT GALIIIAYLT SRADFAAYLH IPNIKGSEEL VIFLGALLGG 

       250        260        270        280        290        300 
SFGFLWFNAY PAKIMMGDTG SLALGAILGM AALILKSEIL FSILAGVFII ETMSVIIQVL 

       310        320        330        340        350 
VYKKTKKRVF KMAPLHHHFE ELGWSEMQVV IRFWIIGLIF AIIALSTIKI R

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Dunn J.J., Butler-Loffredo L., Kieleczawa J., Medalle J., Luft B.J. Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[2]	"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. Venter J.C. Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[3]	"Mapping and sequencing of a locus involved in the cell division of Borrelia burgdorferi." Ge Y., Old I.G., Saint-Girons I., Charon N.W. Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-351. Strain: 212.

Hide | Top

Cross-references

Sequence databases
EMBL GenBank DDBJ	U43739 Genomic DNA. Translation: AAA85626.1. AE000783 Genomic DNA. Translation: AAC66645.1. X96685 Genomic DNA. Translation: CAA65460.1. X96432 Genomic DNA. Translation: CAA65292.1.
PIR	G70137.
RefSeq	NP_212437.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1195140.
GenomeReviews	Gene locus BB_0303 in contig AE000783_GR.
KEGG	bbu:BB0303.
NMPDR	fig\|224326.1.peg.687.
TIGR	BB_0303.
Phylogenomic databases
HOGENOM	HBG708263.
OMA	HHHFEQK.
PhylomeDB	Q44776.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0303-MONOMER.
BRENDA	2.7.8.13. 142596.
Family and domain databases
HAMAP	MF_00038. MraY. [Tree]
InterPro	IPR000715. Glycosyl_transferase_4. IPR018481. Glycosyl_Trfase_4_cons-reg. IPR003524. PNAcMuramoyl-5peptid_Trfase. IPR018480. PNAcMuramoyl-5peptid_Trfase_CS. [Graphical view]
PANTHER	PTHR22926. Glyco_trans_4. 1 hit. PTHR22926:SF3. PNAcPpept_trans. 1 hit.
Pfam	PF00953. Glycos_transf_4. 1 hit. PF10555. MraY_sig1. 1 hit. [Graphical view]
TIGRFAMs	TIGR00445. mraY. 1 hit.
PROSITE	PS01347. MRAY_1. 1 hit. PS01348. MRAY_2. 1 hit. [Graphical view]
ProtoNet	Search...

Hide | Top

Entry information

Entry name

MRAY_BORBU

Accession

Primary (citable) accession number: Q44776
Secondary accession number(s): Q60120

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents