Reviewed,
UniProtKB/Swiss-Prot P09790 (IGA_NEIGO)
Last modified
June 16, 2009.
Version 78.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: IgA-specific serine endopeptidase EC=3.4.21.72 Alternative name(s): IgA protease | ||
| Gene names |
| ||
| Organism | Neisseria gonorrhoeae | ||
| Taxonomic identifier | 485 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria |
Protein attributes
| Sequence length | 1532 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | This protease is specific for immunoglobulin A. |
| Catalytic activity | Cleavage of immunoglobulin A molecules at certain Pro-|-Xaa bonds in the hinge region. No small molecule substrates are known. |
| Subcellular location | |
| Domain | The signal peptide guides the precursor to the periplasmic space, and the C-terminal helper domain associates with the outer membrane to form a pore for excretion of the protease domain. The helper domain is then released by autoproteolysis. |
| Sequence similarities | Contains 1 autotransporter (TC 1.B.12) domain. [View classification] Contains 1 peptidase S6 domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane Secreted |
| Domain | Signal Transmembrane |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Autocatalytic cleavage Zymogen |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW outer membraneInferred from electronic annotation. Source: InterPro |
| Molecular function | serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 27 | 27 | |||||||
| Chain | 28 – 986 | 959 | IgA-specific serine endopeptidase | PRO_0000026968 | |||||
| Propeptide | 987 – 1532 | 546 | Helper peptide | PRO_0000026969 | |||||
Regions | |||||||||
| Domain | 1280 – 1532 | 253 | Autotransporter | ||||||
Sites | |||||||||
| Active site | 278 | 1 | Potential | ||||||
| Site | 986 – 987 | 2 | Cleavage; by autolysis | ||||||
| Site | 1018 – 1019 | 2 | Cleavage; by autolysis | ||||||
| Site | 1121 – 1122 | 2 | Cleavage; by autolysis | ||||||
Experimental info | |||||||||
| Sequence conflict | 326 | 1 | H → N Ref.2 | ||||||
| Sequence conflict | 338 | 1 | H → N Ref.2 | ||||||
| Sequence conflict | 428 | 1 | N → M Ref.2 | ||||||
| Sequence conflict | 532 | 1 | H → N Ref.2 | ||||||
| Sequence conflict | 616 | 1 | I → V Ref.2 | ||||||
| Sequence conflict | 632 | 1 | H → N Ref.2 | ||||||
| Sequence conflict | 668 | 1 | K → N Ref.2 | ||||||
Sequences
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References
| [1] | "Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease." Pohlner J., Halter R., Beyreuther K., Meyer T.F. Nature 325:458-462(1987) [PubMed: 3027577] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: MS11. |
| [2] | "Mosaic-like organization of IgA protease genes in Neisseria gonorrhoeae generated by horizontal genetic exchange in vivo." Halter R., Pohlner J., Meyer T.F. EMBO J. 8:2737-2744(1989) [PubMed: 2511009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-680 AND 957-1256. Strain: MS11. |
| [3] | "Inhibition of IgA1 proteinases from Neisseria gonorrhoeae and Hemophilus influenzae by peptide prolyl boronic acids." Bachovchin W.W., Plaut A.G., Flentke G.R., Lynch M., Kettner C.A. J. Biol. Chem. 265:3738-3743(1990) [PubMed: 2105953] [Abstract] Cited for: ACTIVE SITE. |
Cross-references
Sequence databases | |
|---|---|
| X04835 Genomic DNA. Translation: CAA28538.1. | |
| PIR | A26039. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| TCDB | 1.B.12.3.1. autotransporter-1 (AT-1) family. |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.72. 588. |
Family and domain databases | |
| InterPro | IPR005546. Auto_transptbeta. IPR006315. OM_autotransptr_brl. IPR012332. P22_tailspike. IPR000710. Peptidase_S6. IPR004899. Pertactin. [Graphical view] |
| Gene3D | G3DSA:2.160.20.20. P22_tailspike. 1 hit. |
| Pfam | PF03797. Autotransporter. 1 hit. PF02395. Peptidase_S6. 1 hit. PF03212. Pertactin. 1 hit. [Graphical view] |
| PRINTS | PR00921. IGASERPTASE. |
| TIGRFAMs | TIGR01414. autotrans_barl. 1 hit. |
| PROSITE | PS51208. AUTOTRANSPORTER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| PMAP-CutDB | P09790. |
Entry information
| Entry name | IGA_NEIGO | ||||||||
| Accession | Primary (citable) accession number: P09790 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


