Reviewed, UniProtKB/Swiss-Prot O66465 (MRAY_AQUAE)

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:	aq_053

Organism

Aquifex aeolicus [Complete proteome] [HAMAP]

Taxonomic identifier

63363 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	359 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 inner 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 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 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 – 359	359	Phospho-N-acetylmuramoyl-pentapeptide-transferase HAMAP MF_00038		PRO_0000108772
Regions
	Transmembrane	26 – 46	21	Potential
	Transmembrane	73 – 93	21	Potential
	Transmembrane	100 – 120	21	Potential
	Transmembrane	143 – 163	21	Potential
	Transmembrane	166 – 186	21	Potential
	Transmembrane	197 – 217	21	Potential
	Transmembrane	234 – 254	21	Potential
	Transmembrane	261 – 281	21	Potential
	Transmembrane	287 – 307	21	Potential
	Transmembrane	336 – 356	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	O66465-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: B2D6292EA6EA16D4	FASTA	359	40,341
	10 20 30 40 50 60 MLYQLALLLK DYWFAFNVLK YITFRSFTAV LIAFFLTLVL SPSFINRLRK IQRLFGGYVR 70 80 90 100 110 120 EYTPESHEVK KYTPTMGGIV ILIVVTLSTL LLMRWDIKYT WVVLLSFLSF GTIGFWDDYV 130 140 150 160 170 180 KLKNKKGISI KTKFLLQVLS ASLISVLIYY WADIDTILYF PFFKELYVDL GVLYLPFAVF 190 200 210 220 230 240 VIVGSANAVN LTDGLDGLAI GPAMTTATAL GVVAYAVGHS KIAQYLNIPY VPYAGELTVF 250 260 270 280 290 300 CFALVGAGLG FLWFNSFPAQ MFMGDVGSLS IGASLATVAL LTKSEFIFAV AAGVFVFETI 310 320 330 340 350 SVILQIIYFR WTGGKRLFKR APFHHHLELN GLPEPKIVVR MWIISILLAI IAISMLKLR

References

[1]

"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000657 Genomic DNA. Translation: AAC06418.1.
PIR	F70304.
RefSeq	NP_213025.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1192662.
GenomeReviews	Gene locus aq_053 in contig AE000657_GR.
KEGG	aae:aq_053.
NMPDR	fig|224324.1.peg.40.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O66465.
OMA	HHHFEQK.
Enzyme and pathway databases
BioCyc	AAEO224324:AQ_053-MON.
BRENDA	2.7.8.13. 189781.
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_AQUAE

Accession

Primary (citable) accession number: O66465

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	November 3, 2009
This is version 68 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)