C0Z0P8 (C0Z0P8_LACRE) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Phospho-N-acetylmuramoyl-pentapeptide-transferase HAMAP-Rule MF_00038
EC=2.7.8.13 HAMAP-Rule MF_00038

Alternative name(s):
UDP-MurNAc-pentapeptide phosphotransferase HAMAP-Rule MF_00038

Gene names

Name:	mraY HAMAP-Rule MF_00038 EMBL EEI08559.1
ORF Names:	HMPREF0535_1613 EMBL EEI08559.1

Organism

Lactobacillus reuteri MM2-3 EMBL EEI08559.1

Taxonomic identifier

585517 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus › Lactobacillus reuteri

Protein attributes

Sequence length	303 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-Rule 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-Rule MF_00038
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00038
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_00038.
Sequence similarities	Belongs to the glycosyltransferase 4 family. MraY subfamily. HAMAP-Rule MF_00038
Caution	The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Ontologies

Keywords
Biological process	Cell cycle Cell division HAMAP-Rule MF_00038 Cell shape Cell wall biogenesis/degradation HAMAP-Rule MF_00038 Peptidoglycan synthesis HAMAP-Rule MF_00038
Cellular component	Cell membrane HAMAP-Rule MF_00038 Membrane
Domain	Transmembrane Transmembrane helix HAMAP-Rule MF_00038
Molecular function	Transferase HAMAP-Rule MF_00038 EMBL EEI08559.1
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP 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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Transmembrane	37 – 57	21	Helical; By similarity HAMAP-Rule MF_00038
	Transmembrane	61 – 81	21	Helical; By similarity HAMAP-Rule MF_00038
	Transmembrane	98 – 118	21	Helical; By similarity HAMAP-Rule MF_00038
	Transmembrane	120 – 140	21	Helical; By similarity HAMAP-Rule MF_00038
	Transmembrane	153 – 173	21	Helical; By similarity HAMAP-Rule MF_00038
	Transmembrane	176 – 196	21	Helical; By similarity HAMAP-Rule MF_00038
	Transmembrane	205 – 227	23	Helical; By similarity HAMAP-Rule MF_00038
	Transmembrane	231 – 253	23	Helical; By similarity HAMAP-Rule MF_00038
	Transmembrane	282 – 302	21	Helical; By similarity HAMAP-Rule MF_00038

Sequences

	Sequence		Length	Mass (Da)
	C0Z0P8 [UniParc]. Last modified May 26, 2009. Version 1. Checksum: 702E9CDF428CEAA3	FASTA	303	33,569
	10 20 30 40 50 60 MPSLIKYFRA KKEGQQIRKE GPTWHAKKAG TPTMGGLLFI FSAVVTILWV AAWQGLITNT 70 80 90 100 110 120 LWALLFVLVV YGLIGMWDDS IKIFHHQNEG FKPWQKALCQ VLAAMVFTVI YQHEGFQMGF 130 140 150 160 170 180 GTTQIGWLYG LFIIFWIVGF SNAVNLTDGL DGLVSGLSII SFAAYLIIAL VNLNQPGYPE 190 200 210 220 230 240 IALFCLAMIG TLLGFFPYNH KPAKIFMGDM GSLAIGASLA AVSLLLHHEW SLLVIGIVYV 250 260 270 280 290 300 CETASVILQV ASFKTTGKRI FKMTPIHHHF EMSGWSEWKI DIVFWLVGLV AAIIAVTTIL LVG

References

[1]

Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y. , Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., Worley K., Gibbs R. Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: MM2-3 EMBL EEI08559.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	ACLB01000090 Genomic DNA. Translation: EEI08559.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EEI08559; EEI08559; HMPREF0535_1613.
PATRIC	37024688. VBILacReu127513_1232.
Enzyme and pathway databases
UniPathway	UPA00219.
Family and domain databases
HAMAP	MF_00038. MraY.
InterPro	IPR000715. Glycosyl_transferase_4. IPR003524. PNAcMuramoyl-5peptid_Trfase. IPR018480. PNAcMuramoyl-5peptid_Trfase_CS. [Graphical view]
PANTHER	PTHR22926. PTHR22926. 1 hit. PTHR22926:SF3. PTHR22926:SF3. 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

C0Z0P8_LACRE

Accession

Primary (citable) accession number: C0Z0P8

Entry history

Integrated into UniProtKB/TrEMBL:	May 26, 2009
Last sequence update:	May 26, 2009
Last modified:	April 3, 2013
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)