O53168 · RIPA_MYCTU
- ProteinPeptidoglycan endopeptidase RipA
- GeneripA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids472 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan from a number of Actinobacteria; activity is increased in the presence of RpfB and inhibited by PBP1A (ponA1). Required for normal separation of daughter cells after cell division and for cell wall integrity. Required for host cell invasion and intracellular survival in host macrophages.
Miscellaneous
Was identified as a high-confidence drug target.
Activity regulation
MoxR1-mediated folding is critical for secretion via the TAT system (PubMed:26933057).
The synergistic effects on peptidoglycan degradation of RipA plus RpfB are inhibited by addition of PBP1A (ponA1) (PubMed:20686708).
The synergistic effects on peptidoglycan degradation of RipA plus RpfB are inhibited by addition of PBP1A (ponA1) (PubMed:20686708).
pH Dependence
Optimum pH is between 5 and 5.5.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 383 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 432 | Proton acceptor | ||||
Sequence: H | ||||||
Active site | 444 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | peptidoglycan-based cell wall | |
Molecular Function | cysteine-type peptidase activity | |
Molecular Function | N-acetylmuramoyl-L-alanine amidase activity | |
Biological Process | cell wall organization | |
Biological Process | cell wall organization or biogenesis | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidoglycan endopeptidase RipA
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionO53168
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 382-385 | Abolishes host cell invasion and survival in host macrophages. | ||||
Sequence: DCSG → AAAA | ||||||
Mutagenesis | 383 | Loss of enzyme activity. | ||||
Sequence: C → A | ||||||
Mutagenesis | 419-421 | Abolishes host cell invasion. | ||||
Sequence: RGD → AGA |
Miscellaneous
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-39 | Tat-type signal | ||||
Sequence: MRRNRRGSPARPAARFVRPAIPSALSVALLVCTPGLATA | ||||||
Chain | PRO_0000413762 | 40-472 | Peptidoglycan endopeptidase RipA | |||
Sequence: DPQTDTIAALIADVAKANQRLQDLSDEVQAEQESVNKAMVDVETARDNAAAAEDDLEVSQRAVKDANAAIAAAQHRFDTFAAATYMNGPSVSYLSASSPDEIIATVTAAKTLSASSQAVMANLQRARTERVNTESAARLAKQKADKAAADAKASQDAAVAALTETRRKFDEQREEVQRLAAERDAAQARLQAARLVAWSSEGGQGAPPFRMWDPGSGPAGGRAWDGLWDPTLPMIPSANIPGDPIAVVNQVLGISATSAQVTANMGRKFLEQLGILQPTDTGITNAPAGSAQGRIPRVYGRQASEYVIRRGMSQIGVPYSWGGGNAAGPSKGIDSGAGTVGFDCSGLVLYSFAGVGIKLPHYSGSQYNLGRKIPSSQMRRGDVIFYGPNGSQHVTIYLGNGQMLEAPDVGLKVRVAPVRTAGMTPYVVRYIEY |
Post-translational modification
Exported by the Tat system (PubMed:26933057).
The position of the signal peptide cleavage has not been experimentally proven (PubMed:26933057).
The position of the signal peptide cleavage has not been experimentally proven (PubMed:26933057).
Proteomic databases
Interaction
Subunit
Monomer. Interacts with RpfB and PBP1A (ponA1) via residues 448-472 of RipA, interacts with RpfE (PubMed:17919286, PubMed:20686708, PubMed:20826344, PubMed:21864539).
Interacts with the chaperone MoxR1 (PubMed:26933057).
RipA-MoxR1 interaction in the cytoplasm leads to proper folding of RipA, resulting in its secretion (PubMed:26933057).
Also interacts with Mce2B (PubMed:26933057).
Interacts with the chaperone MoxR1 (PubMed:26933057).
RipA-MoxR1 interaction in the cytoplasm leads to proper folding of RipA, resulting in its secretion (PubMed:26933057).
Also interacts with Mce2B (PubMed:26933057).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 340-472 | NlpC/P60 | ||||
Sequence: RQASEYVIRRGMSQIGVPYSWGGGNAAGPSKGIDSGAGTVGFDCSGLVLYSFAGVGIKLPHYSGSQYNLGRKIPSSQMRRGDVIFYGPNGSQHVTIYLGNGQMLEAPDVGLKVRVAPVRTAGMTPYVVRYIEY |
Sequence similarities
Belongs to the peptidase C40 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length472
- Mass (Da)49,808
- Last updated1998-06-01 v1
- Checksum3B7D83D29E3631DD
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL123456 EMBL· GenBank· DDBJ | CCP44237.1 EMBL· GenBank· DDBJ | Genomic DNA |