Reviewed, UniProtKB/Swiss-Prot Q5P9K3 (MRAY_ANAMM)

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:	AM1207

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	342 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 – 342	342	Phospho-N-acetylmuramoyl-pentapeptide-transferase HAMAP MF_00038		PRO_0000108770
Regions
	Transmembrane	8 – 28	21	Potential
	Transmembrane	58 – 78	21	Potential
	Transmembrane	86 – 106	21	Potential
	Transmembrane	116 – 136	21	Potential
	Transmembrane	152 – 172	21	Potential
	Transmembrane	184 – 204	21	Potential
	Transmembrane	213 – 233	21	Potential
	Transmembrane	242 – 262	21	Potential
	Transmembrane	267 – 287	21	Potential
	Transmembrane	318 – 338	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5P9K3-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 57F6D2807902E3AA	FASTA	342	36,574
	10 20 30 40 50 60 MFSPIGKVAQ PYFCSFLLST ILGFVIAPRT IAALKNIQKG RNPVRSCFPA AHLAKKSGIP 70 80 90 100 110 120 SMGGVIILLP CILSTAIFGD LHDRDIWVIL TTMVAFAILG GVDDYLKFTR QNPQGISLEA 130 140 150 160 170 180 KLFAQLLIAS AALIFLSYTS DSFTSTHIFS KGLIDLGWAY MPFAYIVVVG SSNSVNLTDG 190 200 210 220 230 240 LDGLATLPII TSTAILGIIG HLSLQFGAEP PGVVGANIPI FCSALVGSAL SFLWFNAHPA 250 260 270 280 290 300 QVFMGDLGSL SLGASLGLMS VMLKCEFIYA ISGCIFVAEA ISSMAQVAYC KLTKGRKIFL 310 320 330 340 VAPIHHHFEK AGLKEATIVT RAWVIAMVSF VVSLAAIIYI YR

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000030 Genomic DNA. Translation: AAV87027.1.
RefSeq	YP_154282.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5P9K3.
Genome annotation databases
GeneID	3171695.
GenomeReviews	Gene locus AM1207 in contig CP000030_GR.
KEGG	ama:AM1207.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5P9K3.
OMA	AGGLMFY.
Enzyme and pathway databases
BioCyc	AMAR234826:AM1207-MON.
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_ANAMM

Accession

Primary (citable) accession number: Q5P9K3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	January 4, 2005
Last modified:	November 3, 2009
This is version 40 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)