Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 88 (11 Dec 2019)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Lys-gingipain W83

Gene

kgp

Organism
Porphyromonas gingivalis
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

Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG (PubMed:9245829). Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria (By similarity). Has hemolytic activity; this is mediated by the adhesin domains and does not require the catalytic domain (PubMed:21812842, PubMed:24265933).By similarity2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi313Calcium 1Combined sources1 Publication1
Metal bindingi337Calcium 2Combined sources1 Publication1
Metal bindingi339Calcium 2Combined sources1 Publication1
Metal bindingi341Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi343Calcium 2Combined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei444Proton donor1 Publication1
Active sitei477Nucleophile1 Publication1
Metal bindingi482Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi491Calcium 1Combined sources1 Publication1
Metal bindingi988Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi990Calcium 3Combined sources1 Publication1
Metal bindingi1001Calcium 4Combined sources1 Publication1
Metal bindingi1003Calcium 4Combined sources1 Publication1
Metal bindingi1005Calcium 4Combined sources1 Publication1
Metal bindingi1007Calcium 4; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1022Calcium 3Combined sources1 Publication1
Metal bindingi1024Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1043Calcium 4Combined sources1 Publication1
Metal bindingi1146Calcium 3Combined sources1 Publication1
Metal bindingi1147Calcium 3Combined sources1 Publication1
Metal bindingi1433Calcium 5; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1435Calcium 5Combined sources1 Publication1
Metal bindingi1446Calcium 6Combined sources1 Publication1
Metal bindingi1448Calcium 6Combined sources1 Publication1
Metal bindingi1450Calcium 6Combined sources1 Publication1
Metal bindingi1452Calcium 6; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1470Calcium 5Combined sources1 Publication1
Metal bindingi1472Calcium 5; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1490Calcium 6Combined sources1 Publication1
Metal bindingi1595Calcium 5Combined sources1 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, Protease, Thiol protease
Biological processVirulence
LigandCalcium, Metal-binding

<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:
Lys-gingipain W831 PublicationBy similarity (EC:3.4.22.471 Publication)
Alternative name(s):
Lysine specific cysteine protease1 PublicationImported
Lysine-specific cysteine proteinase1 PublicationImported
Porphypain1 PublicationImported
PrtK481 Publication
Cleaved into the following 4 chains:
Lys-gingipain catalytic subunit1 PublicationBy similarity
39 kDa adhesin1 Publication
Alternative name(s):
PrtK391 Publication
15 kDa adhesin1 Publication
Alternative name(s):
PrtK151 Publication
44 kDa adhesin1 Publication
Alternative name(s):
PrtK441 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
Name:kgpBy similarity
Synonyms:prtKImported, prtP1 PublicationImported
<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>OrganismiPorphyromonas gingivalis
<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 identifieri837 [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 lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

<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 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24Sequence analysisAdd BLAST24
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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_000039538125 – 2281 PublicationAdd BLAST204
<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_0000395382229 – 1732Lys-gingipain W831 PublicationAdd BLAST1504
ChainiPRO_0000395383229 – 680Lys-gingipain catalytic subunit2 PublicationsAdd BLAST452
ChainiPRO_0000395384738 – ?39 kDa adhesin1 Publication
ChainiPRO_00003953851157 – ?15 kDa adhesin1 Publication
ChainiPRO_00003953861292 – ?44 kDa adhesin2 Publications

<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

Proteolytically cleaved into a catalytic subunit and three adhesins. Arg-gingipain is involved in this post-translational processing.1 Publication

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>Sitei228 – 229Cleavage; site 11 Publication2
Sitei737 – 738Cleavage; site 21 Publication2
Sitei1156 – 1157Cleavage; site 31 Publication2
Sitei1291 – 1292Cleavage; site 41 Publication2

Keywords - PTMi

Zymogen

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q51817

<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

11732
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
Q51817

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 general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The isolated adhesin domains have hemolytic activity (in vitro).2 Publications

<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 C25 family.Sequence analysis

Keywords - Domaini

Signal

Family and domain databases

Conserved Domains Database

More...
CDDi
cd10913 Peptidase_C25_N_gingipain, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 4 hits
2.60.40.3800, 1 hit
3.40.50.10390, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029030 Caspase-like_dom_sf
IPR011628 Cleaved_adhesin
IPR001769 Gingipain
IPR039392 Gingipain_N
IPR029031 Gingipain_N_sf
IPR038490 Gingipain_propep_sf
IPR013783 Ig-like_fold
IPR018832 Pept_C25_gingipain_C
IPR005536 Peptidase_C25_Ig-like_domain
IPR012600 Propeptide_C25

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07675 Cleaved_Adhesin, 3 hits
PF10365 DUF2436, 1 hit
PF01364 Peptidase_C25, 1 hit
PF03785 Peptidase_C25_C, 1 hit
PF08126 Propeptide_C25, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52129 SSF52129, 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.

Q51817-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRKLLLLIAA SLLGVGLYAQ SAKIKLDAPT TRTTCTNNSF KQFDASFSFN
60 70 80 90 100
EVELTKVETK GGTFASVSIP GAFPTGEVGS PEVPAVRKLI AVPVGATPVV
110 120 130 140 150
RVKSFTEQVY SLNQYGSEKL MPHQPSMSKS DDPEKVPFVY NAAAYARKGF
160 170 180 190 200
VGQELTQVEM LGTMRGVRIA ALTINPVQYD VVANQLKVRN NIEIEVSFQG
210 220 230 240 250
ADEVATQRLY DASFSPYFET AYKQLFNRDV YTDHGDLYNT PVRMLVVAGA
260 270 280 290 300
KFKEALKPWL TWKAQKGFYL DVHYTDEAEV GTTNASIKAF IHKKYNDGLA
310 320 330 340 350
ASAAPVFLAL VGDTDVISGE KGKKTKKVTD LYYSAVDGDY FPEMYTFRMS
360 370 380 390 400
ASSPEELTNI IDKVLMYEKA TMPDKSYLEK VLLIAGADYS WNSQVGQPTI
410 420 430 440 450
KYGMQYYYNQ EHGYTDVYNY LKAPYTGCYS HLNTGVSFAN YTAHGSETAW
460 470 480 490 500
ADPLLTTSQL KALTNKDKYF LAIGNCCITA QFDYVQPCFG EVITRVKEKG
510 520 530 540 550
AYAYIGSSPN SYWGEDYYWS VGANAVFGVQ PTFEGTSMGS YDATFLEDSY
560 570 580 590 600
NTVNSIMWAG NLAATHAGNI GNITHIGAHY YWEAYHVLGD GSVMPYRAMP
610 620 630 640 650
KTNTYTLPAS LPQNQASYSI QASAGSYVAI SKDGVLYGTG VANASGVATV
660 670 680 690 700
SMTKQITENG NYDVVITRSN YLPVIKQIQV GEPSPYQPVS NLTATTQGQK
710 720 730 740 750
VTLKWEAPSA KKAEGSREVK RIGDGLFVTI EPANDVRANE AKVVLAADNV
760 770 780 790 800
WGDNTGYQFL LDADHNTFGS VIPATGPLFT GTASSNLYSA NFEYLVPANA
810 820 830 840 850
DPVVTTQNII VTGQGEVVIP GGVYDYCITN PEPASGKMWI AGDGGNQPAR
860 870 880 890 900
YDDFTFEAGK KYTFTMRRAG MGDGTDMEVE DDSPASYTYT VYRDGTKIKE
910 920 930 940 950
GLTATTFEED GVAAGNHEYC VEVKYTAGVS PKVCKDVTVE GSNEFAPVQN
960 970 980 990 1000
LTGSSVGQKV TLKWDAPNGT PNPNPNPNPN PGTTLSESFE NGIPASWKTI
1010 1020 1030 1040 1050
DADGDGHGWK PGNAPGIAGY NSNGCVYSES FGLGGIGVLT PDNYLITPAL
1060 1070 1080 1090 1100
DLPNGGKLTF WVCAQDANYA SEHYAVYASS TGNDASNFTN ALLEETITAK
1110 1120 1130 1140 1150
GVRSPKAIRG RIQGTWRQKT VDLPAGTKYV AFRHFQSTDM FYIDLDEVEI
1160 1170 1180 1190 1200
KANGKRADFT ETFESSTHGE APAEWTTIDA DGDGQGWLCL SSGQLDWLTA
1210 1220 1230 1240 1250
HGGSNVVSSF SWNGMALNPD NYLISKDVTG ATKVKYYYAV NDGFPGDHYA
1260 1270 1280 1290 1300
VMISKTGTNA GDFTVVFEET PNGINKGGAR FGLSTEANGA KPQSVWIERT
1310 1320 1330 1340 1350
VDLPAGTKYV AFRHYNCSDL NYILLDDIQF TMGGSPTPTD YTYTVYRDGT
1360 1370 1380 1390 1400
KIKEGLTETT FEEDGVATGN HEYCVEVKYT AGVSPKKCVD VTVNSTQFNP
1410 1420 1430 1440 1450
VQNLTAEQAP NSMDAILKWN APASKRAEVL NEDFENGIPA SWKTIDADGD
1460 1470 1480 1490 1500
GNNWTTTPPP GGSSFAGHNS AICVSSASHI NFEGPQNPDN YLVTPELSLP
1510 1520 1530 1540 1550
GGGTLTFWVC AQDANYASEH YAVYASSTGN DASNFANALL EEVLTAKTVV
1560 1570 1580 1590 1600
TAPEAIRGTR AQGTWYQKTV QLPAGTKYVA FRHFGCTDFF WINLDDVVIT
1610 1620 1630 1640 1650
SGNAPSYTYT IYRNNTQIAS GVTETTYRDP DLATGFYTYG VKVVYPNGES
1660 1670 1680 1690 1700
AIETATLNIT SLADVTAQKP YTLTVVGKTI TVTCQGEAMI YDMNGRRLAA
1710 1720 1730
GRNTVVYTAQ GGHYAVMVVV DGKSYVEKLA VK
Length:1,732
Mass (Da):187,875
Last modified:November 1, 1996 - 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:i654271DBEF7BCAE4
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 conflicti796V → I in AAB60809 (PubMed:10219167).Curated1
Sequence conflicti1351K → N in AAC26523 (PubMed:9632563).Curated1
Sequence conflicti1364D → Y in AAC26523 (PubMed:9632563).Curated1
Sequence conflicti1390D → N in AAB60809 (PubMed:10219167).Curated1
Sequence conflicti1448D → H in AAC26523 (PubMed:9632563).Curated1
Sequence conflicti1479H → Y in AAB60809 (PubMed:10219167).Curated1

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Several forms of kgp with differences at the C-terminus exist in different P.gingivalis strains.1 Publication

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
U42210 Genomic DNA Translation: AAB06565.1
AF017059 Genomic DNA Translation: AAC26523.1
U75366 Genomic DNA Translation: AAB60809.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T30836

<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
U42210 Genomic DNA Translation: AAB06565.1
AF017059 Genomic DNA Translation: AAC26523.1
U75366 Genomic DNA Translation: AAB60809.1
PIRiT30836

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
3M1HX-ray1.56A/B/C/D1427-1602[»]
4ITCX-ray1.55A982-1154[»]
4RBMX-ray1.75A229-683[»]
4TKXX-ray1.60L229-680[»]
5MUNX-ray1.80A/B20-228[»]
6I9AX-ray1.20A/B229-683[»]
SMRiQ51817
ModBaseiSearch...
PDBe-KBiSearch...

Proteomic databases

PRIDEiQ51817

Family and domain databases

CDDicd10913 Peptidase_C25_N_gingipain, 1 hit
Gene3Di2.60.40.10, 4 hits
2.60.40.3800, 1 hit
3.40.50.10390, 1 hit
InterProiView protein in InterPro
IPR029030 Caspase-like_dom_sf
IPR011628 Cleaved_adhesin
IPR001769 Gingipain
IPR039392 Gingipain_N
IPR029031 Gingipain_N_sf
IPR038490 Gingipain_propep_sf
IPR013783 Ig-like_fold
IPR018832 Pept_C25_gingipain_C
IPR005536 Peptidase_C25_Ig-like_domain
IPR012600 Propeptide_C25
PfamiView protein in Pfam
PF07675 Cleaved_Adhesin, 3 hits
PF10365 DUF2436, 1 hit
PF01364 Peptidase_C25, 1 hit
PF03785 Peptidase_C25_C, 1 hit
PF08126 Propeptide_C25, 1 hit
SUPFAMiSSF52129 SSF52129, 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 nameiKGP83_PORGN
<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: Q51817
Secondary accession number(s): O07442, O52050
<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: July 13, 2010
Last sequence update: November 1, 1996
Last modified: December 11, 2019
This is version 88 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
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