Q9WY77 (MRAY_THEMA) Reviewed, UniProtKB/Swiss-Prot

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:	TM_0235

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
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. 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.

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 Transmembrane helix
Molecular function	Transferase
Technical term	Complete proteome Reference 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-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity Inferred from electronic annotation. Source: EC phospho-N-acetylmuramoyl-pentapeptide-transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 302	302	Phospho-N-acetylmuramoyl-pentapeptide-transferase HAMAP MF_00038		PRO_0000108917
Regions
	Transmembrane	1 – 21	21	Helical; Potential
	Transmembrane	42 – 62	21	Helical; Potential
	Transmembrane	67 – 87	21	Helical; Potential
	Transmembrane	95 – 115	21	Helical; Potential
	Transmembrane	123 – 143	21	Helical; Potential
	Transmembrane	154 – 174	21	Helical; Potential
	Transmembrane	178 – 198	21	Helical; Potential
	Transmembrane	204 – 224	21	Helical; Potential
	Transmembrane	229 – 249	21	Helical; Potential
	Transmembrane	279 – 299	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9WY77 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: BB8FF74FEA9205CB	FASTA	302	33,814
	10 20 30 40 50 60 MIAANFLLNL FLYPILIKLF RRRRIGQYIR KEGPDLHGYK EGTPTMGGIL FVLTGFLFGM 70 80 90 100 110 120 ISKTNTMVLL GMFLFFLIGF LDDFLSVARK DSTGLKTYQK ALLQTLAAFI MLLLIRPDTN 130 140 150 160 170 180 VDFFGSTIEM GKWYYLFALL VIVGSSNAMN LTDGLDGLAG WIYVSGSIPY WFFLKERGVS 190 200 210 220 230 240 EDILLILGVG VLAFLVFNSK PAKIFMGDTG SITLGGVLGT VSVLTKTEFY LVLFFMIPVI 250 260 270 280 290 300 ETLSVILQVG SFKIFKRRIF KMSPLHHHFE LIGWSEEKIV AVFTVFNLIS SLVALEIFGV IG

References

[1]

"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000512 Genomic DNA. Translation: AAD35326.1.
PIR	E72402.
RefSeq	NP_228049.1. NC_000853.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	897134.
GenomeReviews	Gene locus TM_0235 in contig AE000512_GR.
KEGG	tma:TM0235.
NMPDR	fig|243274.1.peg.233.
PATRIC	23935345. VBITheMar51294_0238.
TIGR	TM_0235.
Phylogenomic databases
HOGENOM	HBG708263.
OMA	QVGYFKW.
PhylomeDB	Q9WY77.
ProtClustDB	PRK14654.
Enzyme and pathway databases
BioCyc	TMAR243274:TM_0235-MONOMER.
Family and domain databases
HAMAP	MF_00038. MraY. [Tree]
InterPro	IPR000715. Glycosyl_transferase_4. IPR003524. PNAcMuramoyl-5peptid_Trfase. IPR018480. PNAcMuramoyl-5peptid_Trfase_CS. [Graphical view]
KO	K01000.
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_THEMA

Accession

Primary (citable) accession number: Q9WY77

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program