Reviewed, UniProtKB/Swiss-Prot A7Z4E2 (MRAY_BACA2)

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:	RBAM_015050

Organism

Bacillus amyloliquefaciens (strain FZB42) [Complete proteome] [HAMAP]

Taxonomic identifier

326423 [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_1000002937
Regions
	Transmembrane	5 – 25	21	Potential
	Transmembrane	50 – 70	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)
	A7Z4E2-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 2B1A6C6299F29426	FASTA	324	35,384
	10 20 30 40 50 60 MLEQVILFTI IMGFLISVLI SPILIPFLRR LKFGQSIREE GPKSHMKKSG TPTMGGVMII 70 80 90 100 110 120 VSIAITAIVM TQKFSHLSAE MFLLLFVTIG YGLLGFLDDY IKVVMKRNLG LTSKQKLIGQ 130 140 150 160 170 180 IIIAIVFYGV YHYCHFSTGI RVPGTHLSID LGWGYFILVL FMLVGGSNAV NLTDGLDGLL 190 200 210 220 230 240 SGTAAIAFGA FAILAWNQSQ YDVAIFSVAV VGAVLGFLVF NAHPAKVFMG DTGSLALGGA 250 260 270 280 290 300 IVTVAILTKL EILLVIIGGV FVIETLSVIL QVISFKTTGK RIFKMSPLHH HYELVGWSEW 310 320 RVVVTFWTAG LLLAVLGIYI EVWL

References

[1]

"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42." Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R. Nat. Biotechnol. 25:1007-1014(2007) [PubMed: 17704766] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000560 Genomic DNA. Translation: ABS73868.1.
RefSeq	YP_001421099.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A7Z4E2.
Genome annotation databases
GeneID	5461795.
GenomeReviews	Gene locus RBAM_015050 in contig CP000560_GR.
KEGG	bay:RBAM_015050.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	HHHFEQK.
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_BACA2

Accession

Primary (citable) accession number: A7Z4E2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 23, 2007
Last modified:	November 3, 2009
This is version 21 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)