Q83F26 (MRAY_COXBU) 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:	CBU_0125

Organism

Coxiella burnetii

Taxonomic identifier

777 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella

Protein attributes

Sequence length	361 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 – 361	361	Phospho-N-acetylmuramoyl-pentapeptide-transferase HAMAP MF_00038		PRO_0000108816
Regions
	Transmembrane	18 – 38	21	Helical; Potential
	Transmembrane	73 – 93	21	Helical; Potential
	Transmembrane	97 – 117	21	Helical; Potential
	Transmembrane	135 – 155	21	Helical; Potential
	Transmembrane	168 – 188	21	Helical; Potential
	Transmembrane	196 – 216	21	Helical; Potential
	Transmembrane	235 – 255	21	Helical; Potential
	Transmembrane	263 – 283	21	Helical; Potential
	Transmembrane	288 – 308	21	Helical; Potential
	Transmembrane	338 – 358	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q83F26 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 4B74157AA0729276	FASTA	361	39,537
	10 20 30 40 50 60 MLLWLTNFLS QHFHAFRVFN YLTFRSIVSA LTALILVLSL SPRLIKYLVS LQVGQMVRND 70 80 90 100 110 120 GPQTHLKKSG TPTMGGVLII VAIVISVLLW GDLSNRFIWV ILLVTVAFSA IGWMDDYRKI 130 140 150 160 170 180 IRKNSKGLSA RSKYLLQSII GALAAVYLYF SATTGAETAL VIPFLKNVLP NLGLFYIVLA 190 200 210 220 230 240 YFVIVGSSNA VNLTDGLDGL ALMPTVMIGA ALGVFAYTTG NHFFAQYLAI PYIPGAGEVV 250 260 270 280 290 300 VFCSALVGAG LGFLWYNTYP AQVFMGDVGS LGLGAALGVT AVVVRQELVY FLMGGIFVAE 310 320 330 340 350 360 TLSVILQVGY FKLSGGKRIF RMAPLHHHFE LKGWPEPKVI VRFWIITFIL VLCGLATLKL R

References

[1]

"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed: 12704232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nine Mile phase I / RSA 493.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016828 Genomic DNA. Translation: AAO89689.1.
RefSeq	NP_819175.1. NC_002971.3.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1207996.
GenomeReviews	Gene locus CBU_0125 in contig AE016828_GR.
KEGG	cbu:CBU_0125.
NMPDR	fig|227377.1.peg.119.
PATRIC	17928935. VBICoxBur82552_0128.
TIGR	CBU_0125.
Phylogenomic databases
HOGENOM	HBG708263.
OMA	RFWIISM.
PhylomeDB	Q83F26.
ProtClustDB	PRK00108.
Enzyme and pathway databases
BioCyc	CBUR227377:CBU_0125-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_COXBU

Accession

Primary (citable) accession number: Q83F26

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program