Phospho-N-acetylmuramoyl-pentapeptide-transferase

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Reviewed, UniProtKB/Swiss-Prot Q81WC8 (MRAY_BACAN)

Last modified November 3, 2009. Version 51. History...

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

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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:	BA_4052, GBAA_4052, BAS3764

Organism

Bacillus anthracis [Complete proteome] [HAMAP]

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

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Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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General annotation (Comments)

Function	First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan By similarity.
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 membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the glycosyltransferase 4 family. MraY subfamily.

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Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	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 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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 324

324

Phospho-N-acetylmuramoyl-pentapeptide-transferase HAMAP MF_00038

PRO_0000108774

Regions

Transmembrane

5 – 25

Potential

Transmembrane

52 – 72

Potential

Transmembrane

77 – 97

Potential

Transmembrane

122 – 142

Potential

Transmembrane

149 – 169

Potential

Transmembrane

176 – 196

Potential

Transmembrane

201 – 221

Potential

Transmembrane

227 – 247

Potential

Transmembrane

253 – 273

Potential

Transmembrane

302 – 322

Potential

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Sequences

Sequence

Length

Mass (Da)

Tools

Q81WC8-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 7B4A781E303745C2
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FASTA

324

34,941

        10         20         30         40         50         60 
MLEQGLLVTA GVAFLISVAL SPLFIPFLRK LKFGQSIRDE GPKSHQKKSG TPTMGGIVIY 

        70         80         90        100        110        120 
VSMMVTSLIM AIKFNHLGAE VSLLLLVTFG YGLIGFLDDY IKVVKKRNLG LTSKQKLVGQ 

       130        140        150        160        170        180 
LVIAIAFFFI GKGQAFHTYI MIPGTDVKFE LGWAYFVLVL FMLIGGSNAV NLTDGLDGLL 

       190        200        210        220        230        240 
SGTAAIAFGA FSIIAVAQEQ FGVAIFCMAV VGAVLGFLVF NANPAEVFMG DTGSLALGGA 

       250        260        270        280        290        300 
IAAVAILLKQ ELLLVIIGGV FVMETLSVII QVISFKTTGK RVFKMSPLHH HYELCGWSEW 

       310        320 
RVVVTFWSVG FLLAVLGIYI GVWM

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References

[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M. Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.

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Cross-references

Sequence databases
	AE016879 Genomic DNA. Translation: AAP27778.1. AE017334 Genomic DNA. Translation: AAT33169.1. AE017225 Genomic DNA. Translation: AAT56066.1.
RefSeq	NP_846292.1. YP_020694.1. YP_030015.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1087475. 2819653. 2850428.
GenomeReviews	Gene locus BA_4052 in contig AE016879_GR. Gene locus BAS3764 in contig AE017225_GR. Gene locus GBAA_4052 in contig AE017334_GR.
KEGG	ban:BA4052. bar:GBAA4052. bat:BAS3764.
TIGR	BA_4052. GBAA_4052.
Phylogenomic databases
HOGENOM	Q81WC8.
OMA	HHHFEQK.
Enzyme and pathway databases
BioCyc	BANT260799:BAS3764-MON. BANT261594:GBAA4052-MON.
BRENDA	2.7.8.13. 267517.
Family and domain databases
HAMAP	MF_00038. [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. False negative. PS01348. MRAY_2. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

MRAY_BACAN

Accession

Primary (citable) accession number: Q81WC8
Secondary accession number(s): Q6HUH3, Q6KNQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 51 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)

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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

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