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Protein

Phospho-N-acetylmuramoyl-pentapeptide-transferase

Gene

mraY

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31)
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

GO - Molecular functioni

  1. phospho-N-acetylmuramoyl-pentapeptide-transferase activity Source: UniProtKB-HAMAP
  2. UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. cell wall organization Source: UniProtKB-KW
  4. peptidoglycan biosynthetic process Source: UniProtKB-HAMAP
  5. regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciBCER226900:GJEU-3909-MONOMER.
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:BC_3913
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000001417 Componenti: Chromosome

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei5 – 2521HelicalUniRule annotationAdd
BLAST
Transmembranei52 – 7221HelicalUniRule annotationAdd
BLAST
Transmembranei77 – 9721HelicalUniRule annotationAdd
BLAST
Transmembranei122 – 14221HelicalUniRule annotationAdd
BLAST
Transmembranei149 – 16921HelicalUniRule annotationAdd
BLAST
Transmembranei176 – 19621HelicalUniRule annotationAdd
BLAST
Transmembranei201 – 22121HelicalUniRule annotationAdd
BLAST
Transmembranei227 – 24721HelicalUniRule annotationAdd
BLAST
Transmembranei253 – 27321HelicalUniRule annotationAdd
BLAST
Transmembranei302 – 32221HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 324324Phospho-N-acetylmuramoyl-pentapeptide-transferasePRO_0000108776Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi226900.BC3913.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0472.
KOiK01000.
OMAiHESKIVT.
OrthoDBiEOG69GZPZ.

Family and domain databases

HAMAPiMF_00038. MraY.
InterProiIPR000715. Glycosyl_transferase_4.
IPR003524. PNAcMuramoyl-5peptid_Trfase.
IPR018480. PNAcMuramoyl-5peptid_Trfase_CS.
[Graphical view]
PANTHERiPTHR22926. PTHR22926. 1 hit.
PfamiPF00953. Glycos_transf_4. 1 hit.
PF10555. MraY_sig1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00445. mraY. 1 hit.
PROSITEiPS01348. MRAY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q819Q1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEQGLLVTA GVAFLISVAL SPLFIPFLRK LKFGQSIRDE GPKSHQKKSG
60 70 80 90 100
TPTMGGIVIY VSMMVTSLIM AIKFNYLGAE VSLLLLVTFG YGLIGFLDDY
110 120 130 140 150
IKVVKKRNLG LTSKQKLVGQ LVIAIAFFLI GKGQAFHTYI MIPGTDVKFE
160 170 180 190 200
LGWAYFVLVL FMLIGGSNAV NLTDGLDGLL SGTAAIAFGA FSIIAVAQEQ
210 220 230 240 250
FGVAIFCMAV VGAVLGFLVF NANPAKVFMG DTGSLALGGA IAAVAILLKQ
260 270 280 290 300
ELLLVIIGGV FVMETLSVII QVISFKTTGK RVFKMSPLHH HYELCGWSEW
310 320
RVVVTFWSAG FLLAVLGIYI GVWM
Length:324
Mass (Da):34,904
Last modified:May 31, 2003 - v1
Checksum:i2F1B78105FC3855C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP10834.1.
RefSeqiNP_833633.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP10834; AAP10834; BC_3913.
GeneIDi1206258.
KEGGibce:BC3913.
PATRICi32603863. VBIBacCer54481_4035.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP10834.1.
RefSeqiNP_833633.1. NC_004722.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC3913.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP10834; AAP10834; BC_3913.
GeneIDi1206258.
KEGGibce:BC3913.
PATRICi32603863. VBIBacCer54481_4035.

Phylogenomic databases

eggNOGiCOG0472.
KOiK01000.
OMAiHESKIVT.
OrthoDBiEOG69GZPZ.

Enzyme and pathway databases

UniPathwayiUPA00219.
BioCyciBCER226900:GJEU-3909-MONOMER.

Family and domain databases

HAMAPiMF_00038. MraY.
InterProiIPR000715. Glycosyl_transferase_4.
IPR003524. PNAcMuramoyl-5peptid_Trfase.
IPR018480. PNAcMuramoyl-5peptid_Trfase_CS.
[Graphical view]
PANTHERiPTHR22926. PTHR22926. 1 hit.
PfamiPF00953. Glycos_transf_4. 1 hit.
PF10555. MraY_sig1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00445. mraY. 1 hit.
PROSITEiPS01348. MRAY_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 14579 / DSM 31.

Entry informationi

Entry nameiMRAY_BACCR
AccessioniPrimary (citable) accession number: Q819Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 14, 2005
Last sequence update: May 31, 2003
Last modified: January 6, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.