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Entry version 39 (02 Jun 2021)
Sequence version 1 (12 Dec 2006)
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Beta-peptidyl aminopeptidase BapA

Sphingosinicella microcystinivorans
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

Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu. Requires a beta-amino acid at the N-terminus of peptide substrates and cleaves the peptide bond between the N-terminal beta-amino acid and the amino acid at the second position of tripeptidic substrates of the general structure H-betahXaa-Ile-betahTyr-OH according to the following preferences with regard to the side chain of the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing > hydrogen, basic and polar. beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu.

1 Publication


S.microcystinivorans can degrade microcystin, a cyclic, toxic heptapeptide that contains beta-peptidic substructures.1 Publication

<p>This subsection of the <a href="">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by AEBSF (4-(2-aminoethyl)benzenesulfonyl fluoride, Pefabloc SC).1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=39 mM for beta-homoVal-beta-homoAla-beta-homoLeu
  2. KM=41 mM for beta-homoAla-beta-homoLeu
  3. KM=4.4 mM for beta-3homoAla-pNA
  1. Vmax=0.84 µmol/min/mg enzyme with beta-homoVal-beta-homoAla-beta-homoLeu as substrate
  2. Vmax=3.1 µmol/min/mg enzyme with beta-homoAla-beta-homoLeu as substrate
  3. Vmax=0.063 µmol/min/mg enzyme with carnosine as substrate1 Publication
  4. Vmax=0.047 µmol/min/mg enzyme with beta-homoGly-Ile-beta-homoTyr as substrate1 Publication
  5. Vmax=0.45 µmol/min/mg enzyme with beta-homoVal-Ile-beta-homoTyr as substrate1 Publication
  6. Vmax=0.38 µmol/min/mg enzyme with beta-homoVal-Ile-beta-homoTyr as substrate1 Publication
  7. Vmax=0.46 µmol/min/mg enzyme with beta-homoPhe-Ile-beta-homoTyr as substrate1 Publication
  8. Vmax=0.21 µmol/min/mg enzyme with beta-homoTyr-Ile-beta-homoTyr as substrate1 Publication
  9. Vmax=0.040 µmol/min/mg enzyme with beta-homoTrp-Ile-beta-homoTyr as substrate1 Publication
  10. Vmax=0.40 µmol/min/mg enzyme with beta-homoSer-Ile-beta-homoTyr as substrate1 Publication
  11. Vmax=0.050 µmol/min/mg enzyme with beta-homoThr-Ile-beta-homoTyr as substrate1 Publication
  12. Vmax=0.011 µmol/min/mg enzyme with beta-homoHis-Ile-beta-homoTyr as substrate1 Publication
  13. Vmax=0.015 µmol/min/mg enzyme with beta-homoLys-Ile-beta-homoTyr as substrate1 Publication
  14. Vmax=0.011 µmol/min/mg enzyme with beta-homoArg-Ile-beta-homoTyr as substrate1 Publication
  15. Vmax=0.016 µmol/min/mg enzyme with D-beta-homoVal-Ile-beta-homoTyr as substrate1 Publication

pH dependencei

Optimum pH is 10.1 Publication


Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei271NucleophileBy similarity1
Active sitei309Proton donor/acceptorBy similarity1
Active sitei311Proton donor/acceptorBy similarity1

<p>The <a href="">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="">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 functionAminopeptidase, Hydrolase, Protease

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

BRENDAi, 12100

Protein family/group databases

MEROPS protease database


<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="">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:
Beta-peptidyl aminopeptidase BapA1 Publication (EC: Publication)
Cleaved into the following 2 chains:
Beta-peptidyl aminopeptidase BapA alpha subunit1 Publication
Beta-peptidyl aminopeptidase BapA beta subunit1 Publication
<p>This subsection of the <a href="">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>OrganismiSphingosinicella microcystinivoransImported
<p>This subsection of the <a href="">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 identifieri335406 [NCBI]
<p>This subsection of the <a href="">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 lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingosinicella

<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


<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 – 21Sequence analysisAdd BLAST21
<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_000043076522 – 270Beta-peptidyl aminopeptidase BapA alpha subunitBy similarityAdd BLAST249
ChainiPRO_0000430766271 – 396Beta-peptidyl aminopeptidase BapA beta subunitBy similarityAdd BLAST126

<p>This subsection of the <a href="">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

Autoproteolytic processing to generate the alpha and beta subunit is required for self-activation and is proposed to use a similar mechanism as substrate cleavage.By similarity

<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="">'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="">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterooctamer of 4 heterodimers ((alpha:beta)4); each heterodimer is composed of an alpha subunit and a beta subunit processed from the same precursor.

1 Publication

<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

3D structure databases

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


Database of comparative protein structure models


<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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S58 family.Curated

Keywords - Domaini


Family and domain databases

Integrated resource of protein families, domains and functional sites

View protein in InterPro
IPR016117, ArgJ-like_dom_sf
IPR005321, Peptidase_S58_DmpA

The PANTHER Classification System

PTHR36512, PTHR36512, 1 hit

Pfam protein domain database

View protein in Pfam
PF03576, Peptidase_S58, 1 hit

Superfamily database of structural and functional annotation

SSF56266, SSF56266, 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="">length</a> and <a href="">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="">Sequence</a> section indicates if the <a href="">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="">Sequence</a> section indicates if the <a href="">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.

A0MTQ2-1 [UniParc]FASTAAdd to basket
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Mass (Da):41,184
Last modified:December 12, 2006 - v1
<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="">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i52E275E9E33A8C5C

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database


GenBank nucleotide sequence database


DNA Data Bank of Japan; a nucleotide sequence database

Links Updated
EF043283 Genomic DNA Translation: ABK40073.1

<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="">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:
Links Updated
EF043283 Genomic DNA Translation: ABK40073.1

3D structure databases


Protein family/group databases


Enzyme and pathway databases

BRENDAi3.4.11.25, 12100

Family and domain databases

InterProiView protein in InterPro
IPR016117, ArgJ-like_dom_sf
IPR005321, Peptidase_S58_DmpA
PANTHERiPTHR36512, PTHR36512, 1 hit
PfamiView protein in Pfam
PF03576, Peptidase_S58, 1 hit
SUPFAMiSSF56266, SSF56266, 1 hit

MobiDB: a database of protein disorder and mobility annotations


<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 nameiBAPA_SPHMI
<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: A0MTQ2
<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="">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: December 12, 2006
Last modified: June 2, 2021
This is version 39 of the entry and version 1 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


  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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