Reviewed, UniProtKB/Swiss-Prot Q65JY3 (MRAY_BACLD)

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:	BLi01736, BL02240

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.

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...

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_0000108781
Regions
	Transmembrane	5 – 25	21	Potential
	Transmembrane	52 – 72	21	Potential
	Transmembrane	77 – 97	21	Potential
	Transmembrane	117 – 137	21	Potential
	Transmembrane	147 – 167	21	Potential
	Transmembrane	176 – 196	21	Potential
	Transmembrane	203 – 223	21	Potential
	Transmembrane	227 – 247	21	Potential
	Transmembrane	250 – 270	21	Potential
	Transmembrane	302 – 322	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q65JY3-1 [UniParc]. Last modified March 15, 2005. Version 2. Checksum: 42C92A7BAD3D94D3	FASTA	324	35,483
	10 20 30 40 50 60 MLEQVILFTI IMGFLISVLL SPIFIPFLRR LKFGQSIREE GPKSHQKKSG TPTMGGVMII 70 80 90 100 110 120 LSIIATTIVM TMKFSEVSMN MILLLFVTVG YGLLGFLDDY IKVVMKRNLG LTSKQKLIGQ 130 140 150 160 170 180 IVIALVFYAV YHFQGMPTDI RIPGTELSFD FGWIYPVLVI FMLVGGSNAV NLTDGLDGLL 190 200 210 220 230 240 SGTAAIAFGA FAILAWNQSQ YDVAIFAVAV VGAVLGFLVF NAHPAKVFMG DTGSLALGGA 250 260 270 280 290 300 IVTIAILTKL EILLVIIGGV FVIETLSVIL QVISFKTTGK RIFKMSPLHH HYELVGWSEW 310 320 RVVVTFWTAG LLLAVLGIYI EVWL

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017333 Genomic DNA. Translation: AAU40631.1. Different initiation. CP000002 Genomic DNA. Translation: AAU23274.1.
RefSeq	YP_078912.1. YP_091324.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q65JY3.
Genome annotation databases
GeneID	3030886. 3098087.
GenomeReviews	Gene locus BLi01736 in contig AE017333_GR. Gene locus BL02240 in contig CP000002_GR.
KEGG	bld:BLi01736. bli:BL02240.
NMPDR	fig|279010.5.peg.1583.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q65JY3.
OMA	HHHFEQK.
Enzyme and pathway databases
BioCyc	BLIC279010:BL02240-MON.
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. 1 hit. PS01348. MRAY_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MRAY_BACLD

Accession

Primary (citable) accession number: Q65JY3
Secondary accession number(s): Q62VD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	November 3, 2009
This is version 44 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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