P28628 (LEPS_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 101.
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: Signal peptidase I S Short name=SPase I EC=3.4.21.89 Alternative name(s): Leader peptidase I | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 184 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Not essential for cell viability, but required for efficient secretion of many proteins. Ref.7 |
| Catalytic activity | Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins. |
| Subcellular location | |
| Induction | Expressed at the postexponential growth phase; regulated by the degS-degU system. |
| Miscellaneous | B.subtilis contains five chromosomal type I signal peptidases: sipS, sipT, sipU, sipV and sipW. They have different, but overlapping, substrate specificities and have different transcription patterns. |
| Sequence similarities | Belongs to the peptidase S26 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Molecular function | Hydrolase Protease |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | serine-type peptidase 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 184 | 184 | Signal peptidase I S | PRO_0000109499 | |||||
Regions | |||||||||
| Topological domain | 1 – 18 | 18 | Cytoplasmic Potential | ||||||
| Transmembrane | 19 – 39 | 21 | Helical; Potential | ||||||
| Topological domain | 40 – 184 | 145 | Extracellular Potential | ||||||
Sites | |||||||||
| Active site | 43 | 1 | |||||||
| Active site | 83 | 1 | |||||||
Experimental info | |||||||||
| Mutagenesis | 42 | 1 | D → S: No effect. | ||||||
| Mutagenesis | 43 | 1 | S → A or V: Loss of activity. | ||||||
| Mutagenesis | 43 | 1 | S → C or T: Reduced activity. | ||||||
| Mutagenesis | 44 | 1 | M → A: Increased activity. | ||||||
| Mutagenesis | 46 | 1 | P → A: Slightly reduced activity. | ||||||
| Mutagenesis | 47 | 1 | T → A: No effect. | ||||||
| Mutagenesis | 48 | 1 | L → A: Reduced activity. | ||||||
| Mutagenesis | 69 | 1 | G → A: Slightly reduced activity. | ||||||
| Mutagenesis | 70 | 1 | D → A: Slightly reduced activity. | ||||||
| Mutagenesis | 71 | 1 | I → A: Slightly reduced activity. | ||||||
| Mutagenesis | 72 | 1 | V → A: No effect. | ||||||
| Mutagenesis | 74 | 1 | L → A: Reduced activity. | ||||||
| Mutagenesis | 79 | 1 | V → A: No effect. | ||||||
| Mutagenesis | 81 | 1 | Y → A: Reduced activity. | ||||||
| Mutagenesis | 81 | 1 | Y → F: No effect. | ||||||
| Mutagenesis | 83 | 1 | K → A, H or R: Loss of activity. | ||||||
| Mutagenesis | 84 | 1 | R → A: Loss of activity. | ||||||
| Mutagenesis | 84 | 1 | R → H: Strongly reduced activity. | ||||||
| Mutagenesis | 84 | 1 | R → K: No effect. | ||||||
| Mutagenesis | 86 | 1 | I → A: Slightly reduced activity. | ||||||
| Mutagenesis | 87 | 1 | G → A: No effect. | ||||||
| Mutagenesis | 88 | 1 | L → A: Reduced activity. | ||||||
| Mutagenesis | 89 | 1 | P → A: No effect. | ||||||
| Mutagenesis | 90 | 1 | G → A: No effect. | ||||||
| Mutagenesis | 91 | 1 | D → A, E or N: No effect. | ||||||
| Mutagenesis | 141 | 1 | Y → A: No effect. | ||||||
| Mutagenesis | 145 | 1 | G → A: Strongly reduced activity. | ||||||
| Mutagenesis | 146 | 1 | D → A or N: Strongly reduced activity. | ||||||
| Mutagenesis | 146 | 1 | D → E: No effect. | ||||||
| Mutagenesis | 147 | 1 | N → A: Reduced activity. | ||||||
| Mutagenesis | 150 | 1 | N → A: No effect. | ||||||
| Mutagenesis | 151 | 1 | S → A: Reduced activity. | ||||||
| Mutagenesis | 153 | 1 | D → A: Strongly reduced activity. | ||||||
| Mutagenesis | 153 | 1 | D → E or N: Loss of activity. | ||||||
| Mutagenesis | 154 | 1 | S → A: Slightly reduced activity. | ||||||
| Mutagenesis | 155 | 1 | R → A: Reduced activity. | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Signal peptidase I of Bacillus subtilis: patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases." van Dijl J.M., de Jong A., Vehmaanpera J., Venema G., Bron S. EMBO J. 11:2819-2828(1992) [PubMed: 1639057] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / 6GM(AMY). |
| [2] | "The organization of the Bacillus subtilis 168 chromosome region between the spoVA and serA genetic loci, based on sequence data." Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P. Mol. Microbiol. 10:385-395(1993) [PubMed: 7934829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501. |
| [3] | "Identification of the potential active site of the signal peptidase SipS of Bacillus subtilis. Structural and functional similarities with LexA-like proteases." van Dijl J.M., de Jong A., Venema G., Bron S. J. Biol. Chem. 270:3611-3618(1995) [PubMed: 7876097] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS. |
| [4] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [5] | "Bacillus subtilis can modulate its capacity and specificity for protein secretion through temporally controlled expression of the sipS gene for signal peptidase I." Bolhuis A., Sorokin A., Azevedo V., Ehrlich S.D., Braun P.G., de Jong A., Venema G., Bron S., van Dijl J.M. Mol. Microbiol. 22:605-618(1996) [PubMed: 8951809] [Abstract] Cited for: CHARACTERIZATION. |
| [6] | "Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases." Tjalsma H., Bolhuis A., van Roosmalen M.L., Wiegert T., Schumann W., Broekhuizen C.P., Quax W.J., Venema G., Bron S., van Dijl J.M. Genes Dev. 12:2318-2331(1998) [PubMed: 9694797] [Abstract] Cited for: CHARACTERIZATION. |
| [7] | "The role of the membrane-spanning domain of type I signal peptidases in substrate cleavage site selection." Carlos J.L., Paetzel M., Brubaker G., Karla A., Ashwell C.M., Lively M.O., Cao G., Bullinger P., Dalbey R.E. J. Biol. Chem. 275:38813-38822(2000) [PubMed: 10982814] [Abstract] Cited for: FUNCTION OF TRANSMEMBRANE DOMAIN. |
| [8] | "Protein secretion and possible roles for multiple signal peptidases for precursor processing in bacilli." Bron S., Bolhuis A., Tjalsma H., Holsappel S., Venema G., van Dijl J.M. J. Biotechnol. 64:3-13(1998) [PubMed: 9823656] [Abstract] Cited for: REVIEW. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z11847 Genomic DNA. Translation: CAA77871.1. L09228 Genomic DNA. Translation: AAA67478.1. AL009126 Genomic DNA. Translation: CAB14263.1. |
| PIR | S23381. |
| RefSeq | NP_390212.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P28628. |
| SMR | P28628. Positions 35-86. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S26.003. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000001132; EBBACP00000001132; EBBACG00000001130. |
| GeneID | 938944. |
| GenomeReviews | Gene locus BSU23310 in contig AL009126_GR. |
| KEGG | bsu:BSU23310. |
| NMPDR | fig|224308.1.peg.2335. |
| PATRIC | 18976477. VBIBacSub10457_2429. |
Organism-specific databases | |
| GenoList | BSU23310. [Micado] |
Phylogenomic databases | |
| GeneTree | EBGT00070000031959. |
| HOGENOM | HBG596607. |
| OMA | EDEVFIN. |
| PhylomeDB | P28628. |
| ProtClustDB | CLSK862274. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU23310-MONOMER. |
| BRENDA | 3.4.21.89. 700. |
Family and domain databases | |
| InterPro | IPR000223. Pept_S26A_signal_pept_1. IPR019758. Pept_S26A_signal_pept_1_CS. IPR019757. Pept_S26A_signal_pept_1_Lys-AS. IPR019756. Pept_S26A_signal_pept_1_Ser-AS. IPR019759. Peptidase_S24_S26. IPR015927. Peptidase_S24_S26A/B/C. IPR011056. Peptidase_S24_S26A/B/C_b-rbn. [Graphical view] |
| Gene3D | G3DSA:2.10.109.10. Pept_S24_S26_C. 2 hits. |
| KO | K03100. |
| Pfam | PF00717. Peptidase_S24. 1 hit. [Graphical view] |
| PRINTS | PR00727. LEADERPTASE. |
| SUPFAM | SSF51306. Pept_S24_S26_C. 1 hit. |
| TIGRFAMs | TIGR02227. Sigpep_I_bact. 1 hit. |
| PROSITE | PS00501. SPASE_I_1. 1 hit. PS00760. SPASE_I_2. 1 hit. PS00761. SPASE_I_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LEPS_BACSU | ||||||||
| Accession | Primary (citable) accession number: P28628 | ||||||||
| 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 |
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

Clusters with