Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Elastase

Gene

lasB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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

Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase (PubMed:11533066). Autocatalyses processing of its pro-peptide (PubMed:9642203, PubMed:1744034). Processes the pro-peptide of pro-chitin-binding protein (cbpD) (PubMed:9642203). Involved in the pathogenesis of P.aeruginosa infections.4 Publications

<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

  • Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects. EC:3.4.24.26

<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:
  • Ca2+3 PublicationsNote: Binds 1 Ca2+ ion per subunit.3 Publications
  • Zn2+3 PublicationsNote: Binds 1 Zn2+ ion per subunit.3 Publications

<p>This subsection of the ‘Function’ 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 phosphoramidon.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi333Calcium3 Publications1
Metal bindingi337Zinc; catalytic3 Publications1
<p>This subsection of the ‘Function’ 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 sitei3381 Publication1
Metal bindingi341Zinc; catalytic3 Publications1
Metal bindingi361Zinc; catalytic3 Publications1
Metal bindingi369Calcium3 Publications1
Metal bindingi372Calcium3 Publications1
Metal bindingi380Calcium3 Publications1
Metal bindingi382Calcium; via carbonyl oxygen3 Publications1
Active sitei420Proton donor1 Publication1

<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

GO - Biological processi

<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
Biological processVirulence
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-14569
PAER208964:G1FZ6-3794-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.24.26 5087

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M04.005

<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:
Elastase (EC:3.4.24.26)
Alternative name(s):
Neutral metalloproteinase
PAE1 Publication
Pseudolysin
Cleaved into the following chain:
<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:lasB
Ordered Locus Names:PA3724
<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>OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
<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 identifieri208964 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000002438 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

Organism-specific databases

Pseudomonas genome database

More...
PseudoCAPi
PA3724

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Loss of processing of its own pro-peptide and pro-chitin-binding protein CbpD (PubMed:9642203). Loss of processing of pro-aminopeptidase to mature aminopeptidase (PubMed:11533066).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi420H → D or Y: Loss of proteolytic and elastolytic activity; significantly decreased processing of proelastase, proelastase accumulates in the periplasm (in E.coli). 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1075146

Drug and drug target database

More...
DrugBanki
DB02307 N-(1-Carboxy-3-Phenylpropyl)Phenylalanyl-Alpha-Asparagine

<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 – 231 PublicationAdd BLAST23
<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_000043132224 – 498Pro-elastaseAdd BLAST475
<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_000002861624 – 1974 PublicationsAdd BLAST174
ChainiPRO_0000028617198 – 498Elastase4 PublicationsAdd BLAST301

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi227 ↔ 2553 Publications
Disulfide bondi467 ↔ 4942 Publications

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

Made as a membrane-associated pre-pro-protein, which is exported to the periplasm (yielding pro-elastase) with removal of the signal peptide. Under certain conditions pro-elastase can accumulate. The pro-peptide is removed in the periplasm yielding a (mature length) 33 kDa protein, probably by autocatalysis (PubMed:1744034). The pro-peptide probably remains associated with elastase and can be secreted (PubMed:9642203). Further alterations (perhaps processing) seems to be required before secretion into the extracellular space (PubMed:1744034).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei197 – 198Cleavage; by autolysis1 Publication2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Zymogen

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P14756

PRoteomics IDEntifications database

More...
PRIDEi
P14756

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P14756

<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

Optimal protein expression in vivo requires both Zn2+ and Ca2+ during growth (at protein level).2 Publications

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

Monomer.1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
208964.PA3724

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P14756

<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

1498
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P14756

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

More...
SMRi
P14756

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P14756

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105D4Y Bacteria
COG3227 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000272374

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P14756

KEGG Orthology (KO)

More...
KOi
K01399

Identification of Orthologs from Complete Genome Data

More...
OMAi
HKRTTLA

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P14756

Family and domain databases

Conserved Domains Database

More...
CDDi
cd09597 M4_neutral_protease, 1 hit

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>.<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.

P14756-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKVSTLDLL FVAIMGVSPA AFAADLIDVS KLPSKAAQGA PGPVTLQAAV
60 70 80 90 100
GAGGADELKA IRSTTLPNGK QVTRYEQFHN GVRVVGEAIT EVKGPGKSVA
110 120 130 140 150
AQRSGHFVAN IAADLPGSTT AAVSAEQVLA QAKSLKAQGR KTENDKVELV
160 170 180 190 200
IRLGENNIAQ LVYNVSYLIP GEGLSRPHFV IDAKTGEVLD QWEGLAHAEA
210 220 230 240 250
GGPGGNQKIG KYTYGSDYGP LIVNDRCEMD DGNVITVDMN SSTDDSKTTP
260 270 280 290 300
FRFACPTNTY KQVNGAYSPL NDAHFFGGVV FKLYRDWFGT SPLTHKLYMK
310 320 330 340 350
VHYGRSVENA YWDGTAMLFG DGATMFYPLV SLDVAAHEVS HGFTEQNSGL
360 370 380 390 400
IYRGQSGGMN EAFSDMAGEA AEFYMRGKND FLIGYDIKKG SGALRYMDQP
410 420 430 440 450
SRDGRSIDNA SQYYNGIDVH HSSGVYNRAF YLLANSPGWD TRKAFEVFVD
460 470 480 490
ANRYYWTATS NYNSGACGVI RSAQNRNYSA ADVTRAFSTV GVTCPSAL
Length:498
Mass (Da):53,687
Last modified:April 1, 1990 - 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:i4B6AA96A569D9615
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti75Y → T in strain: PA103 and N-10. 1
Natural varianti102Q → R in strain: PA103 and N-10. 1
Natural varianti185T → Y in strain: PA103 and N-10. 1
Natural varianti211K → I in strain: 569B. 1
Natural varianti241S → G in strain: PA103 and N-10. 1
Natural varianti282K → D in strain: PA103 and N-10. 1
Natural varianti325M → V in strain: IFO 3455. 1
Natural varianti471R → S in strain: PA103. 1

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
M19472 Genomic DNA Translation: AAB36615.1
M24531 Genomic DNA Translation: AAA25811.1
AB029328 Genomic DNA Translation: BAB79621.1
AE004091 Genomic DNA Translation: AAG07111.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A32359 HYBSPA

NCBI Reference Sequences

More...
RefSeqi
NP_252413.1, NC_002516.2
WP_003113835.1, NC_002516.2

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAG07111; AAG07111; PA3724

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
880368

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pae:PA3724

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|208964.12.peg.3895

<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
M19472 Genomic DNA Translation: AAB36615.1
M24531 Genomic DNA Translation: AAA25811.1
AB029328 Genomic DNA Translation: BAB79621.1
AE004091 Genomic DNA Translation: AAG07111.1
PIRiA32359 HYBSPA
RefSeqiNP_252413.1, NC_002516.2
WP_003113835.1, NC_002516.2

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
1EZMX-ray1.50A198-498[»]
1U4GX-ray1.40A198-498[»]
3DBKX-ray1.40A198-498[»]
6F8BX-ray1.30A198-498[»]
ProteinModelPortaliP14756
SMRiP14756
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA3724

Chemistry databases

BindingDBiP14756
ChEMBLiCHEMBL1075146
DrugBankiDB02307 N-(1-Carboxy-3-Phenylpropyl)Phenylalanyl-Alpha-Asparagine

Protein family/group databases

MEROPSiM04.005

Proteomic databases

PaxDbiP14756
PRIDEiP14756

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG07111; AAG07111; PA3724
GeneIDi880368
KEGGipae:PA3724
PATRICifig|208964.12.peg.3895

Organism-specific databases

PseudoCAPiPA3724

Phylogenomic databases

eggNOGiENOG4105D4Y Bacteria
COG3227 LUCA
HOGENOMiHOG000272374
InParanoidiP14756
KOiK01399
OMAiHKRTTLA
PhylomeDBiP14756

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14569
PAER208964:G1FZ6-3794-MONOMER
BRENDAi3.4.24.26 5087

Miscellaneous databases

EvolutionaryTraceiP14756
PMAP-CutDBiP14756

Protein Ontology

More...
PROi
PR:P14756

Family and domain databases

CDDicd09597 M4_neutral_protease, 1 hit
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...

<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 nameiELAS_PSEAE
<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: P14756
<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: April 1, 1990
Last sequence update: April 1, 1990
Last modified: December 5, 2018
This is version 161 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, Complete proteome, Direct protein sequencing, Reference proteome

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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again