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UniProtKB - P37585 (MURG_BACSU)
Protein
UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
Gene
murG
Organism
Bacillus subtilis (strain 168)
Status
Functioni
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).
UniRule annotationCatalytic activityi
- di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-α-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-α-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-α-D-glucosaminyl-(1→4)]-N-acetyl-α-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H+ + UDPUniRule annotationEC:2.4.1.227UniRule annotation
: peptidoglycan biosynthesis Pathwayi
This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotationView all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 124 | UDP-N-acetyl-alpha-D-glucosamineUniRule annotation | 1 | |
Binding sitei | 195 | UDP-N-acetyl-alpha-D-glucosamineUniRule annotation | 1 | |
Binding sitei | 295 | UDP-N-acetyl-alpha-D-glucosamineUniRule annotation | 1 |
GO - Molecular functioni
- glycosyltransferase activity Source: GO_Central
- 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 Source: UniProtKB-EC
- undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity Source: UniProtKB-UniRule
GO - Biological processi
- carbohydrate metabolic process Source: InterPro
- cell cycle Source: UniProtKB-KW
- cell division Source: UniProtKB-KW
- cell wall organization Source: UniProtKB-KW
- lipid glycosylation Source: UniProtKB-UniRule
- peptidoglycan biosynthetic process Source: UniProtKB-UniRule
- regulation of cell shape Source: UniProtKB-KW
Keywordsi
Molecular function | Glycosyltransferase, Transferase |
Biological process | Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis |
Enzyme and pathway databases
BioCyci | BSUB:BSU15220-MONOMER |
UniPathwayi | UPA00219 |
Protein family/group databases
CAZyi | GT28, Glycosyltransferase Family 28 |
Names & Taxonomyi
Protein namesi | Recommended name: UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferaseUniRule annotation (EC:2.4.1.227UniRule annotation)Alternative name(s): Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferaseUniRule annotation |
Gene namesi | Name:murGUniRule annotation Ordered Locus Names:BSU15220 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation; Cytoplasmic side UniRule annotation
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cell membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000109143 | 1 – 363 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferaseAdd BLAST | 363 |
Proteomic databases
PaxDbi | P37585 |
PRIDEi | P37585 |
Interactioni
Protein-protein interaction databases
IntActi | P37585, 1 interactor |
STRINGi | 224308.BSU15220 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 10 – 12 | UDP-N-acetyl-alpha-D-glucosamine bindingUniRule annotation | 3 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0707, Bacteria |
InParanoidi | P37585 |
OMAi | QGARRLN |
PhylomeDBi | P37585 |
Family and domain databases
HAMAPi | MF_00033, MurG, 1 hit |
InterProi | View protein in InterPro IPR006009, GlcNAc_MurG IPR007235, Glyco_trans_28_C IPR004276, GlycoTrans_28_N |
Pfami | View protein in Pfam PF04101, Glyco_tran_28_C, 1 hit PF03033, Glyco_transf_28, 1 hit |
TIGRFAMsi | TIGR01133, murG, 1 hit |
i Sequence
Sequence statusi: Complete.
P37585-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MRIAISGGGT GGHIYPALAF IKEVQRRHPN VEFLYIGTEN GLEKKIVERE
60 70 80 90 100
NIPFRSIEIT GFKRKLSFEN VKTVMRFLKG VKKSKSYLAE FKPDAVIGTG
110 120 130 140 150
GYVCGPVVYA AAKMGIPTIV HEQNSLPGIT NKFLSKYVNK VAICFEEAKS
160 170 180 190 200
HFPSEKVVFT GNPRASEVVS IKTGRSLAEF GLSEDKKTVL IFGGSRGAAP
210 220 230 240 250
INRAVIDMQD VLKTRDYQVL YITGEVHYEK VMNELKSKGA ADNMVTKPFL
260 270 280 290 300
HQMPEYLKAI DVIVARAGAT TIAEITALGI PSVLIPSPYV TANHQEVNAR
310 320 330 340 350
SLGQHDAAIV LKETELSGEK LIEALDRIVL NEQTLKEMSE RTKSLGVPDA
360
AARLYSVLEE LKK
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 181 | G → K in CAA45558 (PubMed:1391053).Curated | 1 | |
Sequence conflicti | 270 | T → A in CAA45558 (PubMed:1391053).Curated | 1 | |
Sequence conflicti | 270 | T → A in AAA83968 (PubMed:2556375).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D10602 Genomic DNA Translation: BAA01454.1 X64259 Genomic DNA Translation: CAA45558.1 AL009126 Genomic DNA Translation: CAB13395.2 M31827 Genomic DNA Translation: AAA83968.1 |
PIRi | S25763, JC1275 |
RefSeqi | NP_389405.2, NC_000964.3 WP_003232184.1, NZ_JNCM01000035.1 |
Genome annotation databases
EnsemblBacteriai | CAB13395; CAB13395; BSU_15220 |
GeneIDi | 935929 |
KEGGi | bsu:BSU15220 |
PATRICi | fig|224308.179.peg.1660 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D10602 Genomic DNA Translation: BAA01454.1 X64259 Genomic DNA Translation: CAA45558.1 AL009126 Genomic DNA Translation: CAB13395.2 M31827 Genomic DNA Translation: AAA83968.1 |
PIRi | S25763, JC1275 |
RefSeqi | NP_389405.2, NC_000964.3 WP_003232184.1, NZ_JNCM01000035.1 |
3D structure databases
SMRi | P37585 |
ModBasei | Search... |
Protein-protein interaction databases
IntActi | P37585, 1 interactor |
STRINGi | 224308.BSU15220 |
Protein family/group databases
CAZyi | GT28, Glycosyltransferase Family 28 |
Proteomic databases
PaxDbi | P37585 |
PRIDEi | P37585 |
Genome annotation databases
EnsemblBacteriai | CAB13395; CAB13395; BSU_15220 |
GeneIDi | 935929 |
KEGGi | bsu:BSU15220 |
PATRICi | fig|224308.179.peg.1660 |
Phylogenomic databases
eggNOGi | COG0707, Bacteria |
InParanoidi | P37585 |
OMAi | QGARRLN |
PhylomeDBi | P37585 |
Enzyme and pathway databases
UniPathwayi | UPA00219 |
BioCyci | BSUB:BSU15220-MONOMER |
Family and domain databases
HAMAPi | MF_00033, MurG, 1 hit |
InterProi | View protein in InterPro IPR006009, GlcNAc_MurG IPR007235, Glyco_trans_28_C IPR004276, GlycoTrans_28_N |
Pfami | View protein in Pfam PF04101, Glyco_tran_28_C, 1 hit PF03033, Glyco_transf_28, 1 hit |
TIGRFAMsi | TIGR01133, murG, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | MURG_BACSU | |
Accessioni | P37585Primary (citable) accession number: P37585 Secondary accession number(s): P18578, Q59247 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1994 |
Last sequence update: | June 16, 2009 | |
Last modified: | February 23, 2022 | |
This is version 144 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families