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Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Borrelia duttonii (strain Ly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan.UniRule annotation

Catalytic activityi

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.UniRule annotation

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processCell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospho-N-acetylmuramoyl-pentapeptide-transferaseUniRule annotation (EC:2.7.8.13UniRule annotation)
Alternative name(s):
UDP-MurNAc-pentapeptide phosphotransferaseUniRule annotation
Gene namesi
Name:mraYUniRule annotation
Ordered Locus Names:BDU_306
OrganismiBorrelia duttonii (strain Ly)
Taxonomic identifieri412419 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesBorreliaceaeBorrelia
Proteomesi
  • UP000000611 Componenti: Chromosome

Subcellular locationi

  • Cell inner membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei17 – 37HelicalUniRule annotationAdd BLAST21
Transmembranei61 – 83HelicalUniRule annotationAdd BLAST23
Transmembranei88 – 105HelicalUniRule annotationAdd BLAST18
Transmembranei130 – 150HelicalUniRule annotationAdd BLAST21
Transmembranei158 – 178HelicalUniRule annotationAdd BLAST21
Transmembranei190 – 210HelicalUniRule annotationAdd BLAST21
Transmembranei230 – 250HelicalUniRule annotationAdd BLAST21
Transmembranei254 – 274HelicalUniRule annotationAdd BLAST21
Transmembranei279 – 299HelicalUniRule annotationAdd BLAST21
Transmembranei328 – 348HelicalUniRule annotationAdd BLAST21

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000905941 – 351Phospho-N-acetylmuramoyl-pentapeptide-transferaseAdd BLAST351

Interactioni

Protein-protein interaction databases

STRINGi412419.BDU_306.

Structurei

3D structure databases

SMRiB5RLC9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 4 family. MraY subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CPY. Bacteria.
COG0472. LUCA.
HOGENOMiHOG000275122.
KOiK01000.
OMAiLMSPLHH.
OrthoDBiPOG091H00VH.

Family and domain databases

CDDicd06852. GT_MraY. 1 hit.
HAMAPiMF_00038. MraY. 1 hit.
InterProiView protein in InterPro
IPR000715. Glycosyl_transferase_4.
IPR003524. PNAcMuramoyl-5peptid_Trfase.
IPR018480. PNAcMuramoyl-5peptid_Trfase_CS.
PANTHERiPTHR22926. PTHR22926. 1 hit.
PfamiView protein in Pfam
PF00953. Glycos_transf_4. 1 hit.
TIGRFAMsiTIGR00445. mraY. 1 hit.
PROSITEiView protein in PROSITE
PS01347. MRAY_1. 1 hit.
PS01348. MRAY_2. 1 hit.

Sequencei

Sequence statusi: Complete.

B5RLC9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFCFLGLRLL KYITFRTAYA TIFAFLLALI FGPFIISRLK KLKLDQILRK
60 70 80 90 100
DGPKRHLSEK MGIPTMGGVL IFFCVLVSLF FWIHFFNIYF LIVLFVMVSF
110 120 130 140 150
ACLGFTDDLL KIKRKNSDGL NPKFKIYGQI LFSFISVVML YYFGGEHVSI
160 170 180 190 200
LYFPFFKSLK LDLGILYIPF GMFVLISASN SFNLTDGLDG LAIGLSIVVI
210 220 230 240 250
GALIIIAYLT SRVDFALYLN IPNVKGCEEL VIFLGALLGG SFGFLWFNAY
260 270 280 290 300
PAKIMMGDTG SLSIGAVLGM VALILKSEIL FAILAGVFVV ETLSVIIQVV
310 320 330 340 350
VYKKTKKRVF KMAPLHHHFE ELGWSEMQVV IRFWIIGLIF AILALSTIKI

R
Length:351
Mass (Da):39,558
Last modified:November 4, 2008 - v1
Checksum:i19A99E1AD71F8DC6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000976 Genomic DNA. Translation: ACH93258.1.
RefSeqiWP_012538069.1. NC_011229.1.

Genome annotation databases

EnsemblBacteriaiACH93258; ACH93258; BDU_306.
KEGGibdu:BDU_306.

Similar proteinsi

Entry informationi

Entry nameiMRAY_BORDL
AccessioniPrimary (citable) accession number: B5RLC9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 4, 2008
Last modified: June 7, 2017
This is version 59 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families