UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase

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Q8Z9G9 (MURG_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
EC=2.4.1.227

Alternative name(s):
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase

Gene names

Name:	murG
Ordered Locus Names:	STY0148, t0132

Organism

Salmonella typhi [Complete proteome] [HAMAP]

Taxonomic identifier

90370 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II) By similarity. HAMAP-Rule MF_00033
Catalytic activity	UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. HAMAP-Rule MF_00033
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00033
Subcellular location	Cell inner membrane; Peripheral membrane protein By similarity HAMAP-Rule MF_00033.
Sequence similarities	Belongs to the glycosyltransferase 28 family. MurG 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
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	UDP-N-acetylgalactosamine biosynthetic process Inferred from electronic annotation. Source: InterPro cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW lipid glycosylation Inferred from electronic annotation. Source: HAMAP peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase activity Inferred from electronic annotation. Source: EC carbohydrate binding Inferred from electronic annotation. Source: InterPro undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase 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

Initiator methionine

Removed By similarity

Chain

2 – 355

354

UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase HAMAP-Rule MF_00033

PRO_0000109205

Sequences

Sequence

Length

Mass (Da)

Tools

Q8Z9G9 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4BEE5C401C540855
Show »

FASTA

355

37,821

        10         20         30         40         50         60 
MSGQPKRLMV MAGGTGGHVF PGLAVAHHLM AQGWQVRWLG TSDRMEADLV PKHGIDIDFI 

        70         80         90        100        110        120 
RISGLRGKGV KALLAAPLRI FNAWRQARAI MKRFKPDVVL GMGGYVSGPG GLAAWSLGIP 

       130        140        150        160        170        180 
VVLHEQNGIA GLTNQWLAKI ATTVMQAFPG AFPNAEVVGN PVRTDVLALP LPQVRLAGRD 

       190        200        210        220        230        240 
GPIRVLVVGG SQGARVLNQT MPQVAARLGD TVTIWHQSGK GAQLTVEQAY AGAGQPQHKV 

       250        260        270        280        290        300 
TEFIDGMAAA YAWADVVVCR SGALTVSEIA AAGLPAIFVP FQHKDRQQYW NALPLENAGA 

       310        320        330        340        350 
AKIFEQPQFT VEAVADTLAG WSREALLTMA ERARAVSIPD ATERVASEVS RVART

« Hide

References

[1]

"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18."
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P.

Barrell B.G.
Nature 413:848-852(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT18.

[2]

"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL627265 Genomic DNA. Translation: CAD01285.1. AE014613 Genomic DNA. Translation: AAO67864.1.
RefSeq	NP_804015.1. NC_004631.1.
3D structure databases
ProteinModelPortal	Q8Z9G9.
SMR	Q8Z9G9. Positions 6-354.
ModBase	Search...
Protein-protein interaction databases
STRING	220341.STY0148.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO67864; AAO67864; t0132. CAD01285; CAD01285; CAD01285.
GeneID	1067713.
KEGG	stt:t0132.
PATRIC	18538112. VBISalEnt120419_0148.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0707.
HOGENOM	HOG000218321.
KO	K02563.
OMA	DDHQTKN.
ProtClustDB	PRK00726.
Enzyme and pathway databases
UniPathway	UPA00219.
Family and domain databases
HAMAP	MF_00033. MurG.
InterPro	IPR006009. GlcNAc_MurG. IPR004276. Glyco_trans_28. IPR007235. Glyco_trans_28_C. [Graphical view]
PANTHER	PTHR21015:SF22. PTHR21015:SF22. 1 hit.
Pfam	PF04101. Glyco_tran_28_C. 1 hit. PF03033. Glyco_transf_28. 1 hit. [Graphical view]
TIGRFAMs	TIGR01133. murG. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURG_SALTI

Accession

Primary (citable) accession number: Q8Z9G9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents