UniProtKB - Q8DNZ9 (MURT_STRR6)
Protein
Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT
Gene
murT
Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Status
Functioni
The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide (PubMed:24044435, PubMed:30093673). The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isoglutamine residue (PubMed:30093673).2 Publications
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 annotation2 PublicationsEC:6.3.5.13UniRule annotation2 Publications
Kineticsi
kcat is 4 sec(-1) with lipid II as substrate.1 Publication
- KM=220 µM for lipid II1 Publication
- KM=16 µM for ATP1 Publication
: 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 | 205 | ZincUniRule annotationBy similarity | 1 | |
Metal bindingi | 208 | ZincUniRule annotationBy similarity | 1 | |
Metal bindingi | 227 | ZincUniRule annotationBy similarity | 1 | |
Metal bindingi | 230 | ZincUniRule annotationBy similarity | 1 | |
Active sitei | 355 | 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 | SPNE171101:SPR1443-MONOMER |
UniPathwayi | UPA00219 |
Names & Taxonomyi
Protein namesi | Recommended name: Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurTUniRule annotationCurated (EC:6.3.5.13UniRule annotation2 Publications) |
Gene namesi | Name:murT1 PublicationUniRule annotation Ordered Locus Names:spr1443Imported |
Organismi | Streptococcus pneumoniae (strain ATCC BAA-255 / R6) |
Taxonomic identifieri | 171101 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
Severe depletion of GatD/MurT produces a high proportion of aberrant cells, elongated or bulging.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 59 | K → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 85 | N → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 136 | D → A: Strong decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 139 | D → A: Slight decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 140 | R → A: Strong decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 143 | E → A: No change in activity. 1 Publication | 1 | |
Mutagenesisi | 355 | D → A: Decrease in activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000446945 | 1 – 447 | Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurTAdd BLAST | 447 |
Interactioni
Subunit structurei
Forms a heterodimer with GatD.
UniRule annotation1 PublicationProtein-protein interaction databases
STRINGi | 171101.spr1443 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q8DNZ9 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0770, Bacteria |
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.
Q8DNZ9-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MNLKTTLGLL AGRSSHFVLS RLGRGSTLPG KVALQFDKDI LQSLAKNYEI
60 70 80 90 100
VVVTGTNGKT LTTALTVGIL KEVYGQVLTN PSGANMITGI ATTFLTAKSS
110 120 130 140 150
KTGKNIAVLE IDEASLSRIC DYIQPSLFVI TNIFRDQMDR FGEIYTTYNM
160 170 180 190 200
ILDAIRKVPT ATVLLNGDSP LFYKPTIPNP IEYFGFDLEK GPAQLAHYNT
210 220 230 240 250
EGILCPDCQG ILKYEHNTYA NLGAYICEGC GCKRPDLDYR LTKLVELTNN
260 270 280 290 300
RSRFVIDGQE YGIQIGGLYN IYNALAAVAI ARFLGADSQL IKQGFDKSRA
310 320 330 340 350
VFGRQETFHI GDKECTLVLI KNPVGATQAI EMIKLAPYPF SLSVLLNANY
360 370 380 390 400
ADGIDTSWIW DADFEQITDM DIPEINAGGV RHSEIARRLR VTGYPAEKIT
410 420 430 440
ETSNLEQVLK TIENQDCKHA YILATYTAML EFRELLASRQ IVRKEMN
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE007317 Genomic DNA Translation: AAL00247.1 |
PIRi | B98052 |
RefSeqi | NP_359036.1, NC_003098.1 WP_001050251.1, NC_003098.1 |
Genome annotation databases
EnsemblBacteriai | AAL00247; AAL00247; spr1443 |
KEGGi | spr:spr1443 |
PATRICi | fig|171101.6.peg.1559 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE007317 Genomic DNA Translation: AAL00247.1 |
PIRi | B98052 |
RefSeqi | NP_359036.1, NC_003098.1 WP_001050251.1, NC_003098.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6FQB | X-ray | 3.00 | A/B/C/D | 1-447 | [»] | |
SMRi | Q8DNZ9 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 171101.spr1443 |
Genome annotation databases
EnsemblBacteriai | AAL00247; AAL00247; spr1443 |
KEGGi | spr:spr1443 |
PATRICi | fig|171101.6.peg.1559 |
Phylogenomic databases
eggNOGi | COG0770, Bacteria |
HOGENOMi | CLU_041534_0_0_9 |
OMAi | WLWDVDY |
Enzyme and pathway databases
UniPathwayi | UPA00219 |
BioCyci | SPNE171101:SPR1443-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_STRR6 | |
Accessioni | Q8DNZ9Primary (citable) accession number: Q8DNZ9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 8, 2019 |
Last sequence update: | March 1, 2003 | |
Last modified: | December 2, 2020 | |
This is version 90 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
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families