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Entry version 129 (29 Sep 2021)
Sequence version 2 (15 Dec 1998)
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Protein

Putative DD-carboxypeptidase TP_0574

Gene

TP_0574

Organism
Treponema pallidum (strain Nichols)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).

1 Publication3 Publications

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).

4 Publications

Miscellaneous

A recombinant non-lipidated form (residues 20-434) is recognized by human antisera, indicating the lipidation site is not essential for antigenicity, although the acylated lipopeptide clearly is antigenic (PubMed:1372297, PubMed:10426995). The non-lipidated form binds also penicillin (PubMed:7972112).3 Publications

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+1 PublicationNote: Carboxypeptidase activity is stimulated by zinc (PubMed:7972112). Penicillin-binding is stimulated by zinc (PubMed:12196546).2 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P29723

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Putative DD-carboxypeptidase TP_05741 Publication (EC:3.4.-.-1 Publication)
Alternative name(s):
47 kDa lipoprotein1 Publication
Short name:
Tp471 Publication
Short name:
Tpp471 Publication
47 kDa membrane antigen1 Publication
47-kilodalton major integral membrane immunogen1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Ordered Locus Names:TP_0574
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiTreponema pallidum (strain Nichols)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri243276 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesTreponemataceaeTreponema
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000811 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi24 – 28HHETH → SHETS: Protein still binds ampicillin, in nonlipidated fragment (residues 21-43), crystallized. 1 Publication5
Mutagenesisi119S → C or G: Protein still binds ampicillin and penicillin, in nonlipidated fragment (residues 21-43). 1 Publication1
Mutagenesisi306K → Q: Protein still binds ampicillin, in nonlipidated fragment (residues 21-43). 1 Publication1
Mutagenesisi315C → A: Protein still binds ampicillin, in nonlipidated fragment (residues 21-43). 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB02879, 2,3-Di-O-Sulfo-Alpha-D-Glucopyranose

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 19Add BLAST19
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001820220 – 434Putative DD-carboxypeptidase TP_0574Add BLAST415

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi20N-palmitoyl cysteine2 Publications1
Lipidationi20S-diacylglycerol cysteine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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).4 Publications

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P29723

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Probably a monomer; a non-lipidated construct (residues 22-434) is monomeric in solution but crystallizes as a homodimer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
243276.TPANIC_0574

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P29723

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P29723

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Keywords - Domaini

Signal

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_562301_0_0_12

Identification of Orthologs from Complete Genome Data

More...
OMAi
TRATTNH

Database of Orthologous Groups

More...
OrthoDBi
751593at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.1270, 1 hit
2.60.40.1300, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029220, BP-Tp47_dom_D
IPR029221, PBP-Tp47_A
IPR029218, PBP-Tp47_dom_C
IPR038698, PBP_Tp47_domC_sf
IPR038031, Tp47_mid_C_dom
IPR036154, Tp47_N_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF14889, PBP-Tp47_a, 1 hit
PF14888, PBP-Tp47_c, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF81986, SSF81986, 2 hits
SSF82220, SSF82220, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51257, PROKAR_LIPOPROTEIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P29723-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKVKYALLSA GALQLLVVGC GSSHHETHYG YATLSYADYW AGELGQSRDV
60 70 80 90 100
LLAGNAEADR AGDLDAGMFD AVSRATHGHG AFRQQFQYAV EVLGEKVLSK
110 120 130 140 150
QETEDSRGRK KWEYETDPSV TKMVRASASF QDLGEDGEIK FEAVEGAVAL
160 170 180 190 200
ADRASSFMVD SEEYKITNVK VHGMKFVPVA VPHELKGIAK EKFHFVEDSR
210 220 230 240 250
VTENTNGLKT MLTEDSFSAR KVSSMESPHD LVVDTVGTGY HSRFGSDAEA
260 270 280 290 300
SVMLKRADGS ELSHREFIDY VMNFNTVRYD YYGDDASYTN LMASYGTKHS
310 320 330 340 350
ADSWWKTGRV PRISCGINYG FDRFKGSGPG YYRLTLIANG YRDVVADVRF
360 370 380 390 400
LPKYEGNIDI GLKGKVLTIG GADAETLMDA AVDVFADGQP KLVSDQAVSL
410 420 430
GQNVLSADFT PGTEYTVEVR FKEFGSVRAK VVAQ
Length:434
Mass (Da):47,665
Last modified:December 15, 1998 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB5C2A75D4A8849E0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti239G → V in AAA75016 (PubMed:1372297).Curated1
Sequence conflicti239G → V in AAA75017 (PubMed:1372297).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M88769 Genomic DNA Translation: AAA75016.1
M88769 Genomic DNA Translation: AAA75017.1 Different termination.
AE000520 Genomic DNA Translation: AAC65545.1

Protein sequence database of the Protein Information Resource

More...
PIRi
D71309

NCBI Reference Sequences

More...
RefSeqi
WP_010882021.1, NC_021490.2

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC65545; AAC65545; TP_0574

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
tpa:TP_0574

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88769 Genomic DNA Translation: AAA75016.1
M88769 Genomic DNA Translation: AAA75017.1 Different termination.
AE000520 Genomic DNA Translation: AAC65545.1
PIRiD71309
RefSeqiWP_010882021.1, NC_021490.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O75X-ray1.95A/B20-434[»]
SMRiP29723
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi243276.TPANIC_0574

Chemistry databases

DrugBankiDB02879, 2,3-Di-O-Sulfo-Alpha-D-Glucopyranose

Proteomic databases

PRIDEiP29723

Genome annotation databases

EnsemblBacteriaiAAC65545; AAC65545; TP_0574
KEGGitpa:TP_0574

Phylogenomic databases

HOGENOMiCLU_562301_0_0_12
OMAiTRATTNH
OrthoDBi751593at2

Enzyme and pathway databases

SABIO-RKiP29723

Miscellaneous databases

EvolutionaryTraceiP29723

Family and domain databases

Gene3Di2.60.40.1270, 1 hit
2.60.40.1300, 1 hit
InterProiView protein in InterPro
IPR029220, BP-Tp47_dom_D
IPR029221, PBP-Tp47_A
IPR029218, PBP-Tp47_dom_C
IPR038698, PBP_Tp47_domC_sf
IPR038031, Tp47_mid_C_dom
IPR036154, Tp47_N_sf
PfamiView protein in Pfam
PF14889, PBP-Tp47_a, 1 hit
PF14888, PBP-Tp47_c, 1 hit
SUPFAMiSSF81986, SSF81986, 2 hits
SSF82220, SSF82220, 1 hit
PROSITEiView protein in PROSITE
PS51257, PROKAR_LIPOPROTEIN, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTA47_TREPA
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P29723
Secondary accession number(s): O83584
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: December 15, 1998
Last modified: September 29, 2021
This is version 129 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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