UniProtKB - O53638 (LDT1_MYCTU)
Protein
L,D-transpeptidase 1
Gene
ldtA
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap3-D-Ala4 bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap3 of the donor stem and the side chain of mDap3 of the acceptor stem. Is specific for donor substrates containing a stem tetrapeptide since it cannot use pentapeptide stems. Is thought to play a role in adaptation to the nonreplicative state of M.tuberculosis.2 Publications
Miscellaneous
The peptidoglycan structure of stationary-phase M.tuberculosis is atypical since it contains a majority (80%) of 3->3 cross-links synthesized by L,D-transpeptidases that predominate over the 4->3 cross-links formed by the D,D-transpeptidase activity of classical penicillin-binding proteins (PubMed:18408028). In fact, 3-3 cross-linkages predominate throughout all growth phases and the ratio of 4-3/3-3 linkages does not vary significantly under any growth condition (PubMed:22906310).1 Publication
Activity regulationi
Is irreversibly inactivated by the beta-lactams carbapenems via the formation of a covalent adduct resulting from acylation of the catalytic Cys; ertapenem and imipenem are the most efficient drugs for in vitro LdtMt1 inactivation. Cephalosporins (cefotaxime, cephalothin, and ceftriaxone) also form covalent adducts with LdtMt1, although the acylation reaction was 7- to 1,000-fold slower and leads to elimination of one of the drug side chains. A high drug concentration (360 µM) of ceftriaxone is required for full inhibition of enzyme activity. Is not inhibited by ampicillin.3 Publications
: peptidoglycan biosynthesis Pathwayi
This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.View 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 | 190 | SubstrateBy similarity | 1 | |
Active sitei | 208 | Proton donor/acceptor1 Publication | 1 | |
Active sitei | 226 | Nucleophile1 Publication | 1 | |
Sitei | 226 | Binds to carbapenem drug (covalent) | 1 | |
Binding sitei | 228 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- peptidoglycan L,D-transpeptidase activity Source: MTBBASE
- transferase activity, transferring acyl groups Source: UniProtKB-KW
GO - Biological processi
- cell wall organization Source: UniProtKB-KW
- peptidoglycan-protein cross-linking Source: MTBBASE
- regulation of cell shape Source: UniProtKB-KW
Keywordsi
Molecular function | Acyltransferase, Transferase |
Biological process | Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis |
Enzyme and pathway databases
BioCyci | MetaCyc:G185E-4233-MONOMER MTBH37RV:G185E-4233-MONOMER |
UniPathwayi | UPA00219 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:ldtA Ordered Locus Names:Rv0116c, RVBD_0116c ORF Names:P425_00122 |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv0116c |
Subcellular locationi
- Periplasm Curated
GO - Cellular componenti
- extracellular region Source: MTBBASE
- periplasmic space Source: UniProtKB-SubCell
Keywords - Cellular componenti
PeriplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 28 | Sequence analysisAdd BLAST | 28 | |
ChainiPRO_0000430332 | 29 – 251 | L,D-transpeptidase 1Add BLAST | 223 |
Proteomic databases
PaxDbi | O53638 |
PRIDEi | O53638 |
Expressioni
Inductioni
Up-regulated 17-fold under nutrient starvation.1 Publication
Interactioni
Subunit structurei
Monomer.
1 PublicationProtein-protein interaction databases
STRINGi | 83332.Rv0116c |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | O53638 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 129 – 249 | YkuDAdd BLAST | 121 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 203 – 204 | Substrate bindingBy similarity | 2 | |
Regioni | 224 – 228 | Carbapenem drug binding | 5 |
Domaini
Consists of two domains connected by a short loop, which form a bent shape. The N-terminal domain (residues 32-122) resembles a c-type immunoglobulin (Ig) domain, and the C-terminal contains the catalytic site that is located in a tiny tunnel.1 Publication
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | ENOG4105FF0 Bacteria COG1376 LUCA |
HOGENOMi | HOG000241380 |
OMAi | AVRITWG |
PhylomeDBi | O53638 |
Family and domain databases
Gene3Di | 2.40.440.10, 1 hit |
InterProi | View protein in InterPro IPR041280 Big_10 IPR005490 LD_TPept_cat_dom IPR038063 Transpep_catalytic_dom |
Pfami | View protein in Pfam PF17964 Big_10, 1 hit PF03734 YkuD, 1 hit |
SUPFAMi | SSF141523 SSF141523, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
O53638-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MRRVVRYLSV VVAITLMLTA ESVSIATAAV PPLQPIPGVA SVSPANGAVV
60 70 80 90 100
GVAHPVVVTF TTPVTDRRAV ERSIRISTPH NTTGHFEWVA SNVVRWVPHR
110 120 130 140 150
YWPPHTRVSV GVQELTEGFE TGDALIGVAS ISAHTFTVSR NGEVLRTMPA
160 170 180 190 200
SLGKPSRPTP IGSFHAMSKE RTVVMDSRTI GIPLNSSDGY LLTAHYAVRV
210 220 230 240 250
TWSGVYVHSA PWSVNSQGYA NVSHGCINLS PDNAAWYFDA VTVGDPIEVV
G
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP003248 Genomic DNA Translation: AFN47964.1 AL123456 Genomic DNA Translation: CCP42841.1 JLDD01000001 Genomic DNA Translation: KBJ41222.1 |
RefSeqi | NP_214630.1, NC_000962.3 WP_003400856.1, NZ_NVQJ01000062.1 |
Genome annotation databases
EnsemblBacteriai | AFN47964; AFN47964; RVBD_0116c CCP42841; CCP42841; Rv0116c KBJ41222; KBJ41222; P425_00122 |
GeneIDi | 886900 |
KEGGi | mtu:Rv0116c mtv:RVBD_0116c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP003248 Genomic DNA Translation: AFN47964.1 AL123456 Genomic DNA Translation: CCP42841.1 JLDD01000001 Genomic DNA Translation: KBJ41222.1 |
RefSeqi | NP_214630.1, NC_000962.3 WP_003400856.1, NZ_NVQJ01000062.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4JMN | X-ray | 2.20 | A | 32-251 | [»] | |
4JMX | X-ray | 2.55 | A | 32-251 | [»] | |
5E51 | X-ray | 2.25 | A/B/C/D | 32-251 | [»] | |
5E5L | X-ray | 1.89 | A/B/C/D | 32-251 | [»] | |
SMRi | O53638 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv0116c |
Proteomic databases
PaxDbi | O53638 |
PRIDEi | O53638 |
Genome annotation databases
EnsemblBacteriai | AFN47964; AFN47964; RVBD_0116c CCP42841; CCP42841; Rv0116c KBJ41222; KBJ41222; P425_00122 |
GeneIDi | 886900 |
KEGGi | mtu:Rv0116c mtv:RVBD_0116c |
Organism-specific databases
TubercuListi | Rv0116c |
Phylogenomic databases
eggNOGi | ENOG4105FF0 Bacteria COG1376 LUCA |
HOGENOMi | HOG000241380 |
OMAi | AVRITWG |
PhylomeDBi | O53638 |
Enzyme and pathway databases
UniPathwayi | UPA00219 |
BioCyci | MetaCyc:G185E-4233-MONOMER MTBH37RV:G185E-4233-MONOMER |
Family and domain databases
Gene3Di | 2.40.440.10, 1 hit |
InterProi | View protein in InterPro IPR041280 Big_10 IPR005490 LD_TPept_cat_dom IPR038063 Transpep_catalytic_dom |
Pfami | View protein in Pfam PF17964 Big_10, 1 hit PF03734 YkuD, 1 hit |
SUPFAMi | SSF141523 SSF141523, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LDT1_MYCTU | |
Accessioni | O53638Primary (citable) accession number: O53638 Secondary accession number(s): F2GLR2, I6X8J8, L0T5Q5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 2014 |
Last sequence update: | June 1, 1998 | |
Last modified: | September 18, 2019 | |
This is version 100 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, Complete proteome, Reference proteomeDocuments
- Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references