P15292 (P3P_LACLS) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 107.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: PIII-type proteinase EC=3.4.21.96 Alternative name(s): Cell wall-associated serine proteinase Lactocepin | ||||
| Gene names |
| ||||
| Encoded on | Plasmid pSK111 Ref.1 Plasmid pLACR3 Ref.2 | ||||
| Organism | Lactococcus lactis subsp. cremoris (strain SK11) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 272622 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Lactococcus › ![]() |
Protein attributes
| Sequence length | 1962 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 | Protease which breaks down milk proteins during the growth of the bacteria on milk. |
| Catalytic activity | Endopeptidase activity with very broad specificity, although some subsite preference have been noted, e.g. large hydrophobic residues in the P1 and P4 positions, and Pro in the P2 position. Best known for its action on caseins, although it has been shown to hydrolyze hemoglobin and oxidized insulin B-chain. |
| Subcellular location | Secreted › cell wall; Peptidoglycan-anchor Potential. |
| Sequence similarities | Belongs to the peptidase S8 family. Contains 2 FIVAR domains. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell wall Secreted |
| Domain | Repeat Signal |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Peptidoglycan-anchor Zymogen |
| Technical term | Complete proteome Direct protein sequencing Plasmid |
| Gene Ontology (GO) | |
| Biological_process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular regionInferred from electronic annotation. Source: UniProtKB-KW 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 – 33 | 33 | |||||||
| Propeptide | 34 – 187 | 154 | PRO_0000027095 | ||||||
| Chain | 188 – 1930 | 1743 | PIII-type proteinase | PRO_0000027096 | |||||
| Propeptide | 1931 – 1962 | 32 | Removed by sortase Potential | PRO_0000027097 | |||||
Regions | |||||||||
| Domain | 1589 – 1641 | 53 | FIVAR 1 | ||||||
| Domain | 1691 – 1742 | 52 | FIVAR 2 | ||||||
| Motif | 1927 – 1931 | 5 | LPXTG sorting signal Potential | ||||||
Sites | |||||||||
| Active site | 217 | 1 | Charge relay system By similarity | ||||||
| Active site | 281 | 1 | Charge relay system By similarity | ||||||
| Active site | 620 | 1 | Charge relay system By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1930 | 1 | Pentaglycyl murein peptidoglycan amidated threonine Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 109 | 1 | T → I in AAA03533. Ref.1 | ||||||
| Sequence conflict | 249 | 1 | A → V in AAA03533. Ref.1 | ||||||
| Sequence conflict | 276 | 1 | T → K in AAA03533. Ref.1 | ||||||
| Sequence conflict | 318 | 1 | T → S in AAA03533. Ref.1 | ||||||
| Sequence conflict | 325 | 1 | T → K in AAA03533. Ref.1 | ||||||
| Sequence conflict | 331 | 1 | L → V in AAA03533. Ref.1 | ||||||
| Sequence conflict | 353 | 1 | D → N in AAA03533. Ref.1 | ||||||
| Sequence conflict | 899 | 1 | E → D in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1213 | 1 | T → M in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1251 | 1 | D → H in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1282 | 1 | E → K in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1304 | 1 | N → K in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1313 | 1 | T → K in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1316 – 1318 | 3 | ANE → TNK in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1394 | 1 | T → S in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1448 | 1 | V → E in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1515 | 1 | K → Q in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1523 | 1 | S → A in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1550 | 1 | V → I in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1673 | 1 | A → D in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1685 | 1 | S → P in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1719 | 1 | V → I in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1722 | 1 | A → E in AAA03533. Ref.1 | ||||||
| Sequence conflict | 1859 – 1918 | 60 | Missing in AAA03533. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Primary structure and organization of the gene for a procaryotic, cell envelope-located serine proteinase." Vos P., Simons G., Siezen R.J., de Vos W.M. J. Biol. Chem. 264:13579-13585(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 188-197. |
| [2] | "Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. Mills D.A.Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SK11. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | J04962 Unassigned DNA. Translation: AAA03533.1. Sequence problems. CP000428 Genomic DNA. Translation: ABJ74078.1. |
| RefSeq | YP_796509.1. NC_008505.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 272622.LACR_C42. |
Protein family/group databases | |
| MEROPS | S08.116. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABJ74078; ABJ74078; LACR_C42. |
| GeneID | 4405830. |
| KEGG | llc:LACR_C42. |
| PATRIC | 22286542. VBILacLac38071_0071. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1404. |
| HOGENOM | HOG000068537. |
| KO | K01361. |
| OMA | TSMASPF. |
| ProtClustDB | CLSK586542. |
Enzyme and pathway databases | |
| BioCyc | LLAC272622:GJUG-2653-MONOMER. |
| SABIO-RK | P15292. |
Family and domain databases | |
| Gene3D | 3.40.50.200. 2 hits. |
| InterPro | IPR019948. Gram-positive_anchor. IPR019931. LPXTG-motif_cell_wall_anchor. IPR000209. Peptidase_S8/S53_dom. IPR023827. Peptidase_S8_Asp-AS. IPR022398. Peptidase_S8_His-AS. IPR023828. Peptidase_S8_Ser-AS. IPR015500. Peptidase_S8_subtilisin-rel. IPR010435. Peptidase_S8A_DUF1034. IPR003137. Protease-assoc_domain. [Graphical view] |
| PANTHER | PTHR10795. PTHR10795. 1 hit. |
| Pfam | PF06280. DUF1034. 1 hit. PF00746. Gram_pos_anchor. 1 hit. PF02225. PA. 1 hit. PF00082. Peptidase_S8. 1 hit. [Graphical view] |
| PRINTS | PR00723. SUBTILISIN. |
| SUPFAM | SSF52743. Pept_S8_S53. 1 hit. |
| TIGRFAMs | TIGR01167. LPXTG_anchor. 1 hit. |
| PROSITE | PS50847. GRAM_POS_ANCHORING. 1 hit. PS00136. SUBTILASE_ASP. 1 hit. PS00137. SUBTILASE_HIS. 1 hit. PS00138. SUBTILASE_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | P3P_LACLS | ||||||||
| Accession | Primary (citable) accession number: P15292 Secondary accession number(s): Q02VE4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
