Detail Information for IndEnz0002001282
IED ID IndEnz0002001282
Enzyme Type ID protease001282
Protein Name Putative DD-carboxypeptidase TP_0574
EC 3.4.-.-
47 kDa lipoprotein
Tp47
Tpp47
47 kDa membrane antigen
47-kilodalton major integral membrane immunogen
Gene Name TP_0574
Organism Treponema pallidum (strain Nichols)
Taxonomic Lineage cellular organisms Bacteria Spirochaetes Spirochaetia Spirochaetales Treponemataceae Treponema Treponema pallidum Treponema pallidum subsp. pallidum (syphilis treponeme) Treponema pallidum (strain Nichols)
Enzyme Sequence MKVKYALLSAGALQLLVVGCGSSHHETHYGYATLSYADYWAGELGQSRDVLLAGNAEADRAGDLDAGMFDAVSRATHGHGAFRQQFQYAVEVLGEKVLSKQETEDSRGRKKWEYETDPSVTKMVRASASFQDLGEDGEIKFEAVEGAVALADRASSFMVDSEEYKITNVKVHGMKFVPVAVPHELKGIAKEKFHFVEDSRVTENTNGLKTMLTEDSFSARKVSSMESPHDLVVDTVGTGYHSRFGSDAEASVMLKRADGSELSHREFIDYVMNFNTVRYDYYGDDASYTNLMASYGTKHSADSWWKTGRVPRISCGINYGFDRFKGSGPGYYRLTLIANGYRDVVADVRFLPKYEGNIDIGLKGKVLTIGGADAETLMDAAVDVFADGQPKLVSDQAVSLGQNVLSADFTPGTEYTVEVRFKEFGSVRAKVVAQ
Enzyme Length 434
Uniprot Accession Number P29723
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.-.-
Enzyme Function FUNCTION: A possible D,D-carboxypeptidase, that releases amino acids sequentially from a proteins C-terminus (PubMed:7972112, PubMed:12196546). Has zinc-dependent carboxypeptidase activity on synthetic depsipeptide substrates (PubMed:7972112). May serve to decrease cross-linking of peptidoglycan, promoting the highly sinusous motility of this spirochaete (Probable). Overexpression of the whole protein in E.coli leads to aberrant cell morphology and extrusion of the cytoplasm, while overexpression of a construct with the first 62 resides of the protein fused to PhoA does have this effect, suggesting the whole protein, not the lipoprotein moiety, is toxic (PubMed:7972112). Binds penicillin (PubMed:2647634, PubMed:7972112). Penicillin binding is covalent, does not require lipidation, and is zinc-dependent (PubMed:7972112, PubMed:12196546). While this protein has beta-lactamase activity in vitro, that is probably not its role in vivo, as T.pallidum is very sensitive to penicillin antibiotics (PubMed:12196546). {ECO:0000269|PubMed:12196546, ECO:0000269|PubMed:2647634, ECO:0000269|PubMed:7972112, ECO:0000305|PubMed:7972112}.; FUNCTION: A pathogen-specific membrane antigen (PubMed:2642466, PubMed:1372297). Most abundant of the membrane lipoproteins, only found in pathogenic treponemes, suggesting that it is an important structural moiety in the cell envelope of virulent treponemal subspecies. A lipopeptide corresponding to the first 6 mature residues induces host (human and mouse) cytokine release by monocyte cell lines via TLR2 and CD14; nonlipidated protein does not stimulate host cells (PubMed:10426995). Stimulates host (human) dendritic cell maturation to become MHC class II-positive antigen presenting cells via TLR2, which depends on lipidation; nonlipidated protein does not stimulate maturation (PubMed:11160304). {ECO:0000269|PubMed:10426995, ECO:0000269|PubMed:11160304, ECO:0000269|PubMed:1372297, ECO:0000269|PubMed:2642466}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (25); Chain (1); Helix (7); Lipidation (2); Mutagenesis (4); Sequence conflict (2); Signal peptide (1); Turn (3)
Keywords 3D-structure;Cell inner membrane;Cell membrane;Direct protein sequencing;Hydrolase;Lipoprotein;Membrane;Palmitate;Protease;Reference proteome;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:7972112}; Lipid-anchor {ECO:0000305|PubMed:10426995}.
Modified Residue
Post Translational Modification PTM: The N-terminus is blocked (PubMed:2642466). Present as a doublet of low abundance 48 kDa and high abundance 47 kDa proteins (PubMed:2647634, PubMed:2668192, PubMed:1372297). The longer form is probably due to readthrough of the stop codon; the extra amino acids at the C-terminus would be X-Lys-Arg-Gly-Val-Leu-Ser-Arg-Val-Ser, a peptide antibody against this sequence detects only the 48 kDa form (PubMed:2668192). {ECO:0000269|PubMed:1372297, ECO:0000269|PubMed:2642466, ECO:0000269|PubMed:2647634, ECO:0000269|PubMed:2668192}.
Signal Peptide SIGNAL 1..19
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1O75;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 47,665
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda