UniProtKB - A0A0H3JN63 (GATD_STAAN)
Protein
Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD
Gene
gatD
Organism
Staphylococcus aureus (strain N315)
Status
Functioni
The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide (PubMed:22291598, PubMed:30154570). The GatD subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia. The resulting ammonia molecule is channeled to the active site of MurT (PubMed:22291598).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
- EC:3.5.1.2UniRule annotation1 Publication
pH dependencei
Optimum pH is 7.5-7.8 for isoglutaminyl synthase activity.1 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 |
---|---|---|---|---|
Active sitei | 94 | NucleophileUniRule annotation2 Publications | 1 | |
Binding sitei | 128 | SubstrateUniRule annotationBy similarity | 1 | |
Active sitei | 189 | UniRule annotation | 1 |
GO - Molecular functioni
- carbon-nitrogen ligase activity on lipid II Source: CACAO
- glutaminase activity Source: UniProtKB-EC
GO - Biological processi
- cell wall organization Source: UniProtKB-KW
- cobalamin biosynthetic process Source: InterPro
- glutamine metabolic process Source: UniProtKB-KW
- peptidoglycan biosynthetic process Source: UniProtKB-UniPathway
- regulation of cell shape Source: UniProtKB-KW
Keywordsi
Molecular function | Hydrolase, Ligase |
Biological process | Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis |
Enzyme and pathway databases
BioCyci | SAUR158879:G1G21-1975-MONOMER |
UniPathwayi | UPA00219 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:gatD1 PublicationUniRule annotation Ordered Locus Names:SA1707Imported |
Organismi | Staphylococcus aureus (strain N315) |
Taxonomic identifieri | 158879 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
The gatD-murT double mutant displays susceptibility to diverse carbapenem and cephalosporin beta-lactam antibiotics and shows increased susceptibility to plectasin.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 94 | C → G or S: Cannot use glutamine. Abolishes amidation of lipid II. 2 Publications | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000446941 | 1 – 243 | Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatDAdd BLAST | 243 |
Interactioni
Subunit structurei
Forms a heterodimer with MurT.
UniRule annotation2 PublicationsStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | A0A0H3JN63 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 6 – 197 | GATase cobBQ-typePROSITE-ProRule annotationAdd BLAST | 192 |
Domaini
The GatD/MurT complex has an open, boomerang-shaped conformation in which GatD is docked onto one end of MurT. Both proteins contribute to the catalytic triad.1 Publication
Sequence similaritiesi
Keywords - Domaini
Glutamine amidotransferasePhylogenomic databases
HOGENOMi | CLU_064047_0_0_9 |
OMAi | GTYMHGP |
Family and domain databases
CDDi | cd01750, GATase1_CobQ, 1 hit |
Gene3Di | 3.40.50.880, 1 hit |
HAMAPi | MF_02213, Lipid_II_synth_GatD, 1 hit |
InterProi | View protein in InterPro IPR029062, Class_I_gatase-like IPR017929, CobB/CobQ_GATase IPR033949, CobQ_GATase1 IPR011698, GATase_3 IPR043702, Lipid_II_synth_GatD |
Pfami | View protein in Pfam PF07685, GATase_3, 1 hit |
SUPFAMi | SSF52317, SSF52317, 1 hit |
PROSITEi | View protein in PROSITE PS51274, GATASE_COBBQ, 1 hit |
i Sequence
Sequence statusi: Complete.
A0A0H3JN63-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MHELTIYHFM SDKLNLYSDI GNIIALRQRA KKRNIKVNVV EINETEGITF
60 70 80 90 100
DECDIFFIGG GSDREQALAT KELSKIKTPL KEAIEDGMPG LTICGGYQFL
110 120 130 140 150
GKKYITPDGT ELEGLGILDF YTESKTNRLT GDIVIESDTF GTIVGFENHG
160 170 180 190 200
GRTYHDFGTL GHVTFGYGNN DEDKKEGIHY KNLLGTYLHG PILPKNYEIT
210 220 230 240
DYLLEKACER KGIPFEPKEI DNEAEIQAKQ VLIDRANRQK KSR
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BA000018 Genomic DNA Translation: BAB42977.1 |
RefSeqi | WP_000544969.1, NC_002745.2 |
Genome annotation databases
EnsemblBacteriai | BAB42977; BAB42977; BAB42977 |
GeneIDi | 45575130 |
KEGGi | sau:SA1707 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BA000018 Genomic DNA Translation: BAB42977.1 |
RefSeqi | WP_000544969.1, NC_002745.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6GS2 | X-ray | 2.04 | A/C | 1-243 | [»] | |
6H5E | X-ray | 2.14 | A/C | 1-243 | [»] | |
SMRi | A0A0H3JN63 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Genome annotation databases
EnsemblBacteriai | BAB42977; BAB42977; BAB42977 |
GeneIDi | 45575130 |
KEGGi | sau:SA1707 |
Phylogenomic databases
HOGENOMi | CLU_064047_0_0_9 |
OMAi | GTYMHGP |
Enzyme and pathway databases
UniPathwayi | UPA00219 |
BioCyci | SAUR158879:G1G21-1975-MONOMER |
Family and domain databases
CDDi | cd01750, GATase1_CobQ, 1 hit |
Gene3Di | 3.40.50.880, 1 hit |
HAMAPi | MF_02213, Lipid_II_synth_GatD, 1 hit |
InterProi | View protein in InterPro IPR029062, Class_I_gatase-like IPR017929, CobB/CobQ_GATase IPR033949, CobQ_GATase1 IPR011698, GATase_3 IPR043702, Lipid_II_synth_GatD |
Pfami | View protein in Pfam PF07685, GATase_3, 1 hit |
SUPFAMi | SSF52317, SSF52317, 1 hit |
PROSITEi | View protein in PROSITE PS51274, GATASE_COBBQ, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GATD_STAAN | |
Accessioni | A0A0H3JN63Primary (citable) accession number: A0A0H3JN63 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 8, 2019 |
Last sequence update: | September 16, 2015 | |
Last modified: | December 2, 2020 | |
This is version 27 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-structureDocuments
- 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