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Entry version 119 (11 Dec 2019)
Sequence version 1 (01 Nov 1995)
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Protein

Thermolysin

Gene

nprS

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score:

Annotation score:4 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

Extracellular zinc metalloprotease.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

  • Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe. EC:3.4.24.27

<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

Protein has several cofactor binding sites:

<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>Temperature dependencei

Thermostable. Retains about 45% of its activity after treatment of 90 degrees Celsius for 30 minutes.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi292Calcium 1By similarity1
Metal bindingi294Calcium 1By similarity1
Metal bindingi296Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi373Calcium 2By similarity1
Metal bindingi377Zinc; catalyticPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei378PROSITE-ProRule annotation1
Metal bindingi381Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi401Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi412Calcium 2By similarity1
Metal bindingi412Calcium 3By similarity1
Metal bindingi418Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi420Calcium 2By similarity1
Metal bindingi420Calcium 3By similarity1
Metal bindingi422Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi425Calcium 2By similarity1
Metal bindingi425Calcium 3By similarity1
Metal bindingi429Calcium 4By similarity1
Metal bindingi432Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi435Calcium 4By similarity1
Active sitei466Proton donorPROSITE-ProRule annotation1

<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, Metalloprotease, Protease
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.24.28 623

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M04.001

<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_and_taxonomy_section">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:
Thermolysin (EC:3.4.24.27)
Alternative name(s):
Neutral protease
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
Name:nprS
Synonyms:nprM
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri1422 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

<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

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

<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

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03949 (2-Sulfanyl-3-Phenylpropanoyl)-Phe-Tyr
DB01935 3-{[(1r)-1-Benzyl-2-Sulfanylethyl]Amino}-3-Oxopropanoic Acid
DB02597 [2(R,S)-2-Sulfanylheptanoyl]-Phe-Ala
DB01786 D-Alanine
DB02655 D-Aspartic Acid
DB02517 D-Glutamic Acid
DB03700 D-Threonine
DB04569 Formic Acid Benzyl Ester
DB02325 Isopropyl alcohol
DB03308 L-Leucyl-Hydroxylamine
DB03255 Phenol
DB02669 RB106

<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 – 31Sequence analysisAdd BLAST31
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002861232 – 235Activation peptide2 PublicationsAdd BLAST204
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000028613236 – 551ThermolysinAdd BLAST316

Keywords - PTMi

Zymogen

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P43133

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Is expressed in the stationary phase. Up-regulated by NprA.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

Secondary structure

1551
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
P43133

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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 M4 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.390.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011096 FTP_domain
IPR025711 PepSY
IPR023612 Peptidase_M4
IPR027268 Peptidase_M4/M1_CTD_sf
IPR001570 Peptidase_M4_C_domain
IPR013856 Peptidase_M4_domain

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07504 FTP, 1 hit
PF03413 PepSY, 1 hit
PF01447 Peptidase_M4, 1 hit
PF02868 Peptidase_M4_C, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00730 THERMOLYSIN

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00142 ZINC_PROTEASE, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P43133-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKRKMKMKLV RFGLAAGLAA QVFFLPYNAL ASTEHVTWNQ QFQTPQFISG
60 70 80 90 100
DLLKVNGTSP EELVYQYVEK NENKFKFHEN AKDTLQLKEK KNDNLGFTFM
110 120 130 140 150
RFQQTYKGIP VFGAVVTAHV KDGTLTALSG TLIPNLDTKG SLKSGKKLSE
160 170 180 190 200
KQARDIAEKD LVANVTKEVP EYEQGKDTEF VVYVNGDEAS LAYVVNLNFL
210 220 230 240 250
TPEPGNWLYI IDAVDGKILN KFNQLDAAKP GDVKSITGTS TVGVGRGVLG
260 270 280 290 300
DQKNINTTYS TYYYLQDNTR GNGIFTYDAK YRTTLPGSLW ADADNQFFAS
310 320 330 340 350
YDAPAVDAHY YAGVTYDYYK NVHNRLSYDG NNAAIRSSVH YSQGYNNAFW
360 370 380 390 400
NGSQMVYGDG DGQTFIPLSG GIDVVAHELT HAVTDYTAGL IYQNESGAIN
410 420 430 440 450
EAISDIFGTL VEFYANKNPD WEIGEDVYTP GISGDSLRSM SDPAKYGDPD
460 470 480 490 500
HYSKRYTGTQ DNGGVHINSG IINKAAYLIS QGGTHYGVSV VGIGRDKLGK
510 520 530 540 550
IFYRALTQYL TPTSNFSQLR AAAVQSATDL YGSTSQEVAS VKQAFDAVGV

K
Length:551
Mass (Da):60,617
Last modified:November 1, 1995 - 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="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFCF4B2B5A7870129
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 conflicti10 – 14VRFGL → RSFGV AA sequence (PubMed:2203733).Curated5
Sequence conflicti24Missing in AAB02774 (PubMed:2203733).Curated1
Sequence conflicti29 – 33ALAST → RLASS AA sequence (PubMed:2203733).Curated5
Sequence conflicti114A → Q in AAB02774 (PubMed:2203733).Curated1
Sequence conflicti124T → S in AAB02774 (PubMed:2203733).Curated1
Sequence conflicti134P → PIP AA sequence (PubMed:2203733).Curated1
Sequence conflicti261T → S in AAB02774 (PubMed:2203733).Curated1
Sequence conflicti463G → A in AAB02774 (PubMed:2203733).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
M21663 Genomic DNA Translation: AAB02774.1
M34237 Genomic DNA Translation: AAA22625.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A46564
B36706

<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
M21663 Genomic DNA Translation: AAB02774.1
M34237 Genomic DNA Translation: AAA22625.1
PIRiA46564
B36706

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
5DLHX-ray2.25A236-551[»]
5ONPX-ray1.34A236-551[»]
5ONQX-ray1.17A236-551[»]
5WR2X-ray2.00A236-551[»]
5WR3X-ray2.10A236-551[»]
5WR4X-ray2.10A236-551[»]
5WR5X-ray1.90A236-551[»]
5WR6X-ray2.30A236-551[»]
6FHPX-ray1.70C/D490-551[»]
6FSMX-ray1.39A236-551[»]
6GHXX-ray1.16A236-551[»]
SMRiP43133
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

DrugBankiDB03949 (2-Sulfanyl-3-Phenylpropanoyl)-Phe-Tyr
DB01935 3-{[(1r)-1-Benzyl-2-Sulfanylethyl]Amino}-3-Oxopropanoic Acid
DB02597 [2(R,S)-2-Sulfanylheptanoyl]-Phe-Ala
DB01786 D-Alanine
DB02655 D-Aspartic Acid
DB02517 D-Glutamic Acid
DB03700 D-Threonine
DB04569 Formic Acid Benzyl Ester
DB02325 Isopropyl alcohol
DB03308 L-Leucyl-Hydroxylamine
DB03255 Phenol
DB02669 RB106

Protein family/group databases

MEROPSiM04.001

Proteomic databases

PRIDEiP43133

Enzyme and pathway databases

BRENDAi3.4.24.28 623

Family and domain databases

Gene3Di1.10.390.10, 1 hit
InterProiView protein in InterPro
IPR011096 FTP_domain
IPR025711 PepSY
IPR023612 Peptidase_M4
IPR027268 Peptidase_M4/M1_CTD_sf
IPR001570 Peptidase_M4_C_domain
IPR013856 Peptidase_M4_domain
PfamiView protein in Pfam
PF07504 FTP, 1 hit
PF03413 PepSY, 1 hit
PF01447 Peptidase_M4, 1 hit
PF02868 Peptidase_M4_C, 1 hit
PRINTSiPR00730 THERMOLYSIN
PROSITEiView protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiTHER_GEOSE
<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: P43133
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: December 11, 2019
This is version 119 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

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Peptidase families
    Classification of peptidase families and list of entries
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