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Entry version 77 (22 Apr 2020)
Sequence version 1 (01 Jul 2008)
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Protein

Lys-gingipain

Gene

kgp

Organism
Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
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. 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.2 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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by the thiol-reducing agents cysteine, 2-mercaptoethanol and dithiothreitol. Inhibited by idoacetamide, idoacetic acid, leupeptin, tosyl-L-lysine and tosyl-L-phenylalanine. Not inhibited by elastatinal, chymostatin, cystatins, alpha1-antichymotrypsin or the serine protease inhibitors phenylmethylsulfonyl fluoride and diisopropylfluorophosphate. Not inhibited by metal ion chelators. Inhibited by the heavy metal ions Fe3+, Zn2+, Cu2+ and Mn2+.1 Publication

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

Optimum pH is 7.5. Activity remains high from pH 6.5 to 9.5. Loses 60% of its activity following incubation at pH 3.5 for 5 minutes.1 Publication

Temperature dependencei

Only retains 40% of activity after incubation at 60 degrees Celsius for 10 minutes.1 Publication

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 1By similarity1
Metal bindingi337Calcium 2By similarity1
Metal bindingi339Calcium 2By similarity1
Metal bindingi341Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi343Calcium 2By similarity1
<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 donorBy similarity1
Active sitei477Nucleophile1 Publication1
Metal bindingi482Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi491Calcium 1By similarity1
Metal bindingi987Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi989Calcium 3By similarity1
Metal bindingi1000Calcium 4By similarity1
Metal bindingi1002Calcium 4By similarity1
Metal bindingi1004Calcium 4By similarity1
Metal bindingi1006Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi1021Calcium 3By similarity1
Metal bindingi1023Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi1042Calcium 4By similarity1
Metal bindingi1145Calcium 3By similarity1
Metal bindingi1146Calcium 3By similarity1
Metal bindingi1430Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi1432Calcium 5By similarity1
Metal bindingi1444Calcium 6By similarity1
Metal bindingi1446Calcium 6By similarity1
Metal bindingi1448Calcium 6By similarity1
Metal bindingi1450Calcium 6; via carbonyl oxygenBy similarity1
Metal bindingi1480Calcium 5By similarity1
Metal bindingi1495Calcium 6By similarity1
Metal bindingi1585Calcium 5By similarity1

<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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
PGIN431947:G1G2V-1940-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.22.47 756

<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-gingipain1 Publication (EC:3.4.22.472 Publications)
Alternative name(s):
Lysine-specific cysteine proteinase Kgp1 PublicationImported
Cleaved into the following 4 chains:
Lys-gingipain catalytic subunit1 PublicationBy similarity
39 kDa adhesinBy similarity
15 kDa adhesinBy similarity
44 kDa adhesinBy similarity
<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:kgpImported
Ordered Locus Names:PGN_1728
<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 (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
<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 identifieri431947 [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 subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000008842 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi476 – 477CC → AA: Loss of activity. 1 Publication2
Mutagenesisi476C → A: No effect on activity. 1 Publication1
Mutagenesisi477C → A: Loss of activity. 1 Publication1

Miscellaneous databases

Pathogen-Host Interaction database

More...
PHI-basei
PHI:7889

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3308977

<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_000039538725 – 228Sequence analysisBy similarityAdd 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_0000395388229 – 1723Lys-gingipainBy similarityAdd BLAST1495
ChainiPRO_0000395389229 – ?Lys-gingipain catalytic subunitBy similarity
ChainiPRO_0000395390738 – ?39 kDa adhesinBy similarity
ChainiPRO_00003953911156 – ?15 kDa adhesinBy similarity
ChainiPRO_00003953921291 – ?44 kDa adhesinBy similarity

<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 (By similarity).By similarity

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 1By similarity2
Sitei737 – 738Cleavage; site 2By similarity2
Sitei1155 – 1156Cleavage; site 3By similarity2
Sitei1290 – 1291Cleavage; site 4By similarity2

Keywords - PTMi

Zymogen

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
B2RLK2

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
431947.PGN_1728

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

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

More...
SMRi
B2RLK2

Database of comparative protein structure models

More...
ModBasei
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 C25 family.Sequence analysis

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4106QXG Bacteria
ENOG410YH82 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_240727_0_0_10

KEGG Orthology (KO)

More...
KOi
K19237

Family and domain databases

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
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.

B2RLK2-1 [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 ALLIAGADSY WNPKIGQQTI
410 420 430 440 450
KYAVQYYYNQ DHGYTDVYSY PKAPYTGCYS HLNTGVGFAN YTAHGSETSW
460 470 480 490 500
ADPSLTATQV KALTNKDKYF LAIGNCCVTA QFDYPQPCFG EVMTRVKEKG
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
NMTKQITENG NYDVVITRSN YLPVIKQIQA GEPSPYQPVS NLTATTQGQK
710 720 730 740 750
VTLKWDAPSA KKAEASREVK RIGDGLFVTI EPANDVRANE AKVVLAADNV
760 770 780 790 800
WGDNTGYQFL LDADHNTFGS VIPATGPLFT GTASSNLYSA NFEYLIPANA
810 820 830 840 850
DPVVTTQNII VTGQGEVVIP GGVYDYCITN PEPASGKMWI AGDGGNQPAR
860 870 880 890 900
YDDFTFEAGK KYTFTMRRAG MGDGTDMEVE DDSPASYTYT VYRDGTKIQE
910 920 930 940 950
GLTATTFEED GVAAGNHEYC VEVKYTAGVS PKVCKDVTVE GSNEFAPVQN
960 970 980 990 1000
LTGSAVGQKV TLKWDAPNGT PNPNPNPNPG TTTLSESFEN GIPASWKTID
1010 1020 1030 1040 1050
ADGDGHGWKP GNAPGIAGYN SNGCVYSESF GLGGIGVLTP DNYLITPALD
1060 1070 1080 1090 1100
LPNGGKLTFW VCAQDANYAS EHYAVYASST GNDASNFTNA LLEETITAKG
1110 1120 1130 1140 1150
VRSPEAIRGR IQGTWRQKTV DLPAGTKYVA FRHFQSTDMF YIDLDEVEIK
1160 1170 1180 1190 1200
ANGKRADFTE TFESSTHGEA PAEWTTIDAD GDGQDWLCLS SGQLDWLTAH
1210 1220 1230 1240 1250
GGTNVVASFS WNGMALNPDN YLISKDVTGA TKVKYYYAVN DGFPGDHYAV
1260 1270 1280 1290 1300
MISKTGTNAG DFTVVFEETP NGINKGGARF GLSTEANGAK PQSVWIERTV
1310 1320 1330 1340 1350
DLPAGTKYVA FRHYNCSDLN YILLDDIQFT MGGSPTPTDY TYTVYRDGTK
1360 1370 1380 1390 1400
IKEGLTETTF EEDGVATGNH EYCVEVKYTA GVSPKVCVNV TINPTQFNPV
1410 1420 1430 1440 1450
KNLKAQPDGG DVVLKWEAPS GKRGELLNED FEGDAIPTGW TALDADGDGN
1460 1470 1480 1490 1500
NWDITLNEFT RGERHVLSPL RASNVAISYS SLLQGQEYLP LTPNNFLITP
1510 1520 1530 1540 1550
KVEGAKKITY KVGSPGLPQW SHDHYALCIS KSGTAAADFE VIFEETMTYT
1560 1570 1580 1590 1600
QGGANLTREK DLPAGTKYVA FRHYNCTDVL GIMIDDVVIT GEGEGPSYTY
1610 1620 1630 1640 1650
TVYRDGTKIQ EGLTETTYRD AGMSAQSHEY CVEVKYAAGV SPKVCVDYIP
1660 1670 1680 1690 1700
DGVADVTAQK PYTLTVVGKT ITVTCQGEAM IYDMNGRRLA AGRNTVVYTA
1710 1720
QGGYYAVMVV VDGKSYVEKL AIK
Length:1,723
Mass (Da):187,262
Last modified:July 1, 2008 - 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:i5628963D251493EB
GO

<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
AP009380 Genomic DNA Translation: BAG34247.1

NCBI Reference Sequences

More...
RefSeqi
WP_012458488.1, NZ_CP025930.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
BAG34247; BAG34247; PGN_1728

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29256891

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pgn:PGN_1728

<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
AP009380 Genomic DNA Translation: BAG34247.1
RefSeqiWP_012458488.1, NZ_CP025930.1

3D structure databases

SMRiB2RLK2
ModBaseiSearch...

Protein-protein interaction databases

STRINGi431947.PGN_1728

Chemistry databases

ChEMBLiCHEMBL3308977

Proteomic databases

PRIDEiB2RLK2

Genome annotation databases

EnsemblBacteriaiBAG34247; BAG34247; PGN_1728
GeneIDi29256891
KEGGipgn:PGN_1728

Phylogenomic databases

eggNOGiENOG4106QXG Bacteria
ENOG410YH82 LUCA
HOGENOMiCLU_240727_0_0_10
KOiK19237

Enzyme and pathway databases

BioCyciPGIN431947:G1G2V-1940-MONOMER
BRENDAi3.4.22.47 756

Miscellaneous databases

PHI-baseiPHI:7889

Family and domain databases

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
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 nameiKGP_PORG3
<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: B2RLK2
<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: July 1, 2008
Last modified: April 22, 2020
This is version 77 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

Documents

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