UniProtKB - A0A0H2WZQ7 (MURT_STAAC)
Protein
Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT
Gene
murT
Organism
Staphylococcus aureus (strain COL)
Status
Functioni
The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide (PubMed:22303291). The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isoglutamine residue (By similarity).By similarity1 Publication
Catalytic activityi
- ATP + β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H2O + L-glutamine = ADP + β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + H+ + L-glutamate + phosphateUniRule annotationBy similarityEC:6.3.5.13UniRule annotationBy similarity
: peptidoglycan biosynthesis Pathwayi
This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotation1 PublicationView 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 |
---|---|---|---|---|
Metal bindingi | 202 | ZincUniRule annotationBy similarity | 1 | |
Metal bindingi | 205 | ZincUniRule annotationBy similarity | 1 | |
Metal bindingi | 224 | ZincUniRule annotationBy similarity | 1 | |
Metal bindingi | 226 | ZincUniRule annotationBy similarity | 1 | |
Active sitei | 349 | UniRule annotationBy similarity | 1 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-UniRule
- carbon-nitrogen ligase activity on lipid II Source: UniProtKB-UniRule
- zinc ion binding Source: UniProtKB-UniRule
GO - Biological processi
- cell wall organization Source: UniProtKB-KW
- peptidoglycan biosynthetic process Source: UniProtKB-UniRule
- regulation of cell shape Source: UniProtKB-KW
Keywordsi
Molecular function | Ligase |
Biological process | Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis |
Ligand | ATP-binding, Metal-binding, Nucleotide-binding, Zinc |
Enzyme and pathway databases
BioCyci | SAUR93062:G1G4B-2143-MONOMER |
UniPathwayi | UPA00219 |
Names & Taxonomyi
Protein namesi | Recommended name: Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurTUniRule annotationCurated (EC:6.3.5.13UniRule annotationBy similarity) |
Gene namesi | Name:murT1 PublicationUniRule annotation Ordered Locus Names:SACOL1951Imported |
Organismi | Staphylococcus aureus (strain COL) |
Taxonomic identifieri | 93062 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
The gatD-murT double mutant shows abnormal peptidoglycan composition, with decreased amidation of the glutamate residue. The mutant has a normal morphology but growth rate is greatly reduced. Mutant shows reduced antibiotic resistance and increased sensitivity to lysozyme.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000446943 | 1 – 437 | Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurTAdd BLAST | 437 |
Interactioni
Subunit structurei
Forms a heterodimer with GatD.
UniRule annotation1 PublicationProtein-protein interaction databases
STRINGi | 93062.SACOL1951 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
HOGENOMi | CLU_041534_0_0_9 |
OMAi | WLWDVDY |
Family and domain databases
HAMAPi | MF_02214, Lipid_II_synth_MurT, 1 hit |
InterProi | View protein in InterPro IPR043703, Lipid_II_synth_MurT IPR036565, Mur-like_cat_sf IPR013221, Mur_ligase_cen IPR013564, MurT_C |
Pfami | View protein in Pfam PF08353, DUF1727, 1 hit PF08245, Mur_ligase_M, 1 hit |
SUPFAMi | SSF53623, SSF53623, 1 hit |
i Sequence
Sequence statusi: Complete.
A0A0H2WZQ7-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MRQWTAIHLA KLARKASRAV GKRGTDLPGQ IARKVDTDIL RKLAEQVDDI
60 70 80 90 100
VFISGTNGKT TTSNLIGHTL KANNIQIIHN NEGANMAAGI TSAFIMQSTP
110 120 130 140 150
KTKIAVIEID EGSIPRVLKE VTPSMMVFTN FFRDQMDRFG EIDIMVNNIA
160 170 180 190 200
ETISNKGIKL LLNADDPFVS RLKIASDTIV YYGMKAHAHE FEQSTMNESR
210 220 230 240 250
YCPNCGRLLQ YDYIHYNQIG HYHCQCGFKR EQAKYEISSF DVAPFLYLNI
260 270 280 290 300
NDEKYDMKIA GDFNAYNALA AYTVLRELGL NEQTIKNGFE TYTSDNGRMQ
310 320 330 340 350
YFKKERKEAM INLAKNPAGM NASLSVGEQL EGEKVYVISL NDNAADGRDT
360 370 380 390 400
SWIYDADFEK LSKQQIEAII VTGTRAEELQ LRLKLAEVEV PIIVERDIYK
410 420 430
ATAKTMDYKG FTVAIPNYTS LAPMLEQLNR SFEGGQS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000046 Genomic DNA Translation: AAW38392.1 |
RefSeqi | WP_001250336.1, NC_002951.2 |
Genome annotation databases
EnsemblBacteriai | AAW38392; AAW38392; SACOL1951 |
GeneIDi | 45575131 |
KEGGi | sac:SACOL1951 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000046 Genomic DNA Translation: AAW38392.1 |
RefSeqi | WP_001250336.1, NC_002951.2 |
3D structure databases
SMRi | A0A0H2WZQ7 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 93062.SACOL1951 |
Genome annotation databases
EnsemblBacteriai | AAW38392; AAW38392; SACOL1951 |
GeneIDi | 45575131 |
KEGGi | sac:SACOL1951 |
Phylogenomic databases
HOGENOMi | CLU_041534_0_0_9 |
OMAi | WLWDVDY |
Enzyme and pathway databases
UniPathwayi | UPA00219 |
BioCyci | SAUR93062:G1G4B-2143-MONOMER |
Family and domain databases
HAMAPi | MF_02214, Lipid_II_synth_MurT, 1 hit |
InterProi | View protein in InterPro IPR043703, Lipid_II_synth_MurT IPR036565, Mur-like_cat_sf IPR013221, Mur_ligase_cen IPR013564, MurT_C |
Pfami | View protein in Pfam PF08353, DUF1727, 1 hit PF08245, Mur_ligase_M, 1 hit |
SUPFAMi | SSF53623, SSF53623, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MURT_STAAC | |
Accessioni | A0A0H2WZQ7Primary (citable) accession number: A0A0H2WZQ7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 8, 2019 |
Last sequence update: | September 16, 2015 | |
Last modified: | December 2, 2020 | |
This is version 28 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Documents
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families