UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase 1 - Bacillus thuringiensis subsp. konkukian (strain 97-27)

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Q6HEQ4 (MURG1_BACHK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. 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 1
EC=2.4.1.227

Alternative name(s):
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase 1

Gene names

Name:	murG1
Ordered Locus Names:	BT9727_3652

Organism

Bacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]

Taxonomic identifier

281309 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
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 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 MF_00033
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00033
Subcellular location	Cell membrane; Peripheral membrane protein By similarity HAMAP MF_00033.
Sequence similarities	Belongs to the glycosyltransferase 28 family. MurG subfamily.
Sequence caution	The sequence AAT61602.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	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 cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW lipid glycosylation Inferred from electronic annotation. Source: InterPro peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW 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: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 364

364

UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase 1 HAMAP MF_00033

PRO_0000225027

Sequences

Sequence

Length

Mass (Da)

Tools

Q6HEQ4 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 6715DD2E1F74F54B
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FASTA

364

39,630

        10         20         30         40         50         60 
MRVLVSGGGT GGHIYPALAL IREIKKLNPE ARFLYIGTEN GLESTIVPKT GIPFQSIVIS 

        70         80         90        100        110        120 
GFKRKISLDN VKTVMRFLKG VQDSKRYIRR FNPDIVIGTG GYVCGPVVYA AAKLGIPTIV 

       130        140        150        160        170        180 
HEQNSVPGVT NKFLSRYVDK VAVCFEAAAE HFPQSKVVMT GNPRASEVMD QNGMKGKRSV 

       190        200        210        220        230        240 
GLSLPKKSVL IFGGSRGARP INDAFVEAIE QFGNKSYEIL YVTGEVHYDK VMEAVKQKGN 

       250        260        270        280        290        300 
PNNVIIKPFI HNMPEVLTGV DLVVSRAGAT TLAELTALGK PSVLIPSPYV TNNHQEKNAR 

       310        320        330        340        350        360 
SVVDKGAAKM LLEKDLTAET LIRDIDEILL DAQTLQNMKL AAGQLGIPDA ANKLYEVMNK 


LVKK

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References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis."
Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P.

Gilna P.
J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT61602.1. Different initiation.
RefSeq	YP_037972.2. NC_005957.1.
3D structure databases
ProteinModelPortal	Q6HEQ4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000075150; EBBACP00000073236; EBBACG00000075141.
GeneID	2856045.
GenomeReviews	Gene locus BT9727_3652 in contig AE017355_GR.
KEGG	btk:BT9727_3652.
NMPDR	fig\|281309.1.peg.3612.
PATRIC	18988330. VBIBacThu119411_3891.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000001194.
HOGENOM	HBG617076.
OMA	EDHQTKN.
ProtClustDB	PRK00726.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_3652-MONOMER.
Family and domain databases
HAMAP	MF_00033. MurG. [Tree]
InterPro	IPR006009. GlcNAc_MurG. IPR004276. Glyco_trans_28. IPR007235. Glyco_trans_28_C. [Graphical view]
KO	K02563.
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

MURG1_BACHK

Accession

Primary (citable) accession number: Q6HEQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	March 7, 2006
Last modified:	January 25, 2012
This is version 61 of the entry and version 2 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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents