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

Serralysin

Gene
N/A
Organism
Serratia marcescens (strain ATCC 21074 / E-15)
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

Naturally present in the silkworm intestine and allows the emerging moth to dissolve its cocoon.

Miscellaneous

The Gly-rich repeats may be important in the extracellular secretion of this metalloprotease.
In Japan this enzyme, isolated from a Serratia strain presents in the gut of silkworms, is used as a food supplement because it is reported to induces fibrinolytic, anti-inflammatory and anti-edemic (prevents swelling and fluid retention) activity in a number of tissues.

<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 of bonds with hydrophobic residues in P1'. EC:3.4.24.40

<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:

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 bindingi192Zinc; catalytic1
<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 sitei1931
Metal bindingi196Zinc; catalytic1
Metal bindingi202Zinc; catalytic1
Metal bindingi232Zinc; catalytic1
Metal bindingi269Calcium 1; via carbonyl oxygen1
Metal bindingi271Calcium 1; via carbonyl oxygen1
Metal bindingi273Calcium 11
Metal bindingi301Calcium 11
Metal bindingi303Calcium 1; via carbonyl oxygen1
Metal bindingi304Calcium 2; via carbonyl oxygen1
Metal bindingi306Calcium 11
Metal bindingi306Calcium 21
Metal bindingi343Calcium 2; via carbonyl oxygen1
Metal bindingi345Calcium 21
Metal bindingi350Calcium 3; via carbonyl oxygen1
Metal bindingi352Calcium 3; via carbonyl oxygen1
Metal bindingi354Calcium 31
Metal bindingi359Calcium 4; via carbonyl oxygen1
Metal bindingi361Calcium 4; via carbonyl oxygen1
Metal bindingi363Calcium 41
Metal bindingi367Calcium 3; via carbonyl oxygen1
Metal bindingi368Calcium 5; via carbonyl oxygen1
Metal bindingi369Calcium 3; via carbonyl oxygen1
Metal bindingi372Calcium 31
Metal bindingi372Calcium 51
Metal bindingi376Calcium 4; via carbonyl oxygen1
Metal bindingi377Calcium 6; via carbonyl oxygen1
Metal bindingi378Calcium 4; via carbonyl oxygen1
Metal bindingi379Calcium 6; via carbonyl oxygen1
Metal bindingi381Calcium 41
Metal bindingi381Calcium 61
Metal bindingi385Calcium 5; via carbonyl oxygen1
Metal bindingi386Calcium 7; via carbonyl oxygen1
Metal bindingi387Calcium 5; via carbonyl oxygen1
Metal bindingi388Calcium 7; via carbonyl oxygen1
Metal bindingi390Calcium 51
Metal bindingi390Calcium 71
Metal bindingi399Calcium 61
Metal bindingi406Calcium 61
Metal bindingi416Calcium 71

<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

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M10.051

<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:
Serralysin (EC:3.4.24.40)
Alternative name(s):
Extracellular metalloproteinase
Serratiopeptidase
Short name:
Serrapeptase
Short name:
Serrapeptidase
Zinc proteinase
<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>OrganismiSerratia marcescens (strain ATCC 21074 / E-15)
<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 identifieri617 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeSerratia

<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 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 <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_00000286951 – 161 PublicationAdd BLAST16
<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_000002869617 – 487SerralysinAdd BLAST471

Keywords - PTMi

Zymogen

<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

1487
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1SRPX-ray2.00A17-487[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P07268

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

More...
SMRi
P07268

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
P07268

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati348 – 365Hemolysin-type calcium-binding 1Add BLAST18
Repeati366 – 383Hemolysin-type calcium-binding 2Add BLAST18

<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 M10B family.Curated

Keywords - Domaini

Repeat

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04277 ZnMc_serralysin_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.150.10.10, 1 hit
3.40.390.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR018511 Hemolysin-typ_Ca-bd_CS
IPR001343 Hemolysn_Ca-bd
IPR024079 MetalloPept_cat_dom_sf
IPR001818 Pept_M10_metallopeptidase
IPR016294 Pept_M10B
IPR013858 Peptidase_M10B_C
IPR006026 Peptidase_Metallo
IPR034033 Serralysin-like
IPR011049 Serralysin-like_metalloprot_C

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00353 HemolysinCabind, 1 hit
PF00413 Peptidase_M10, 1 hit
PF08548 Peptidase_M10_C, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001205 Peptidase_M10B, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00235 ZnMc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51120 SSF51120, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00330 HEMOLYSIN_CALCIUM, 1 hit
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.

P07268-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQSTKKAIEI TESNFAAATT GYDAVDDLLH YHERGNGIQI NGKDSFSNEQ
60 70 80 90 100
AGLFITRENQ TWNGYKVFGQ PVKLTFSFPD YKFSSTNVAG DTGLSKFSAE
110 120 130 140 150
QQQQAKLSLQ SWADVANITF TEVAAGQKAN ITFGNYSQDR PGHYDYGTQA
160 170 180 190 200
YAFLPNTIWQ GQDLGGQTWY NVNQSNVKHP ATEDYGRQTF THEIGHALGL
210 220 230 240 250
SHPGDYNAGE GNPTYRDVTY AEDTRQFSLM SYWSETNTGG DNGGHYAAAP
260 270 280 290 300
LLDDIAAIQH LYGANLSTRT GDTVYGFNSN TGRDFLSTTS NSQKVIFAAW
310 320 330 340 350
DAGGNDTFDF SGYTANQRIN LNEKSFSDVG GLKGNVSIAA GVTIENAIGG
360 370 380 390 400
SGNDVIVGNA ANNVLKGGAG NDVLFGGGGA DELWGGAGKD IFVFSAASDS
410 420 430 440 450
APGASDWIRD FQKGIDKIDL SFFNKEAQSS DFIHFVDHFS GAAGEALLSY
460 470 480
NASNNVTDLS VNIGGHQAPD FLVKIVGQVD VATDFIV
Length:487
Mass (Da):52,235
Last modified:June 20, 2003 - 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:i270A315CADD568C3
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA27738 differs from that shown. Reason: Frameshift at positions 350 and 355.Curated

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
X04127 Genomic DNA Translation: CAA27738.1 Frameshift.

Protein sequence database of the Protein Information Resource

More...
PIRi
A23596 HYSE15

<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
X04127 Genomic DNA Translation: CAA27738.1 Frameshift.
PIRiA23596 HYSE15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SRPX-ray2.00A17-487[»]
ProteinModelPortaliP07268
SMRiP07268
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM10.051

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP07268

Family and domain databases

CDDicd04277 ZnMc_serralysin_like, 1 hit
Gene3Di2.150.10.10, 1 hit
3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR018511 Hemolysin-typ_Ca-bd_CS
IPR001343 Hemolysn_Ca-bd
IPR024079 MetalloPept_cat_dom_sf
IPR001818 Pept_M10_metallopeptidase
IPR016294 Pept_M10B
IPR013858 Peptidase_M10B_C
IPR006026 Peptidase_Metallo
IPR034033 Serralysin-like
IPR011049 Serralysin-like_metalloprot_C
PfamiView protein in Pfam
PF00353 HemolysinCabind, 1 hit
PF00413 Peptidase_M10, 1 hit
PF08548 Peptidase_M10_C, 1 hit
PIRSFiPIRSF001205 Peptidase_M10B, 1 hit
SMARTiView protein in SMART
SM00235 ZnMc, 1 hit
SUPFAMiSSF51120 SSF51120, 1 hit
PROSITEiView protein in PROSITE
PS00330 HEMOLYSIN_CALCIUM, 1 hit
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 nameiPRZN_SERME
<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: P07268
<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, 1988
Last sequence update: June 20, 2003
Last modified: December 5, 2018
This is version 124 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

Documents

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