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Protein

Signal peptidase I S

Gene

sipS

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Not essential for cell viability, but required for efficient secretion of many proteins.1 Publication

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.

Catalytic activityi

Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei431
Active sitei831

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase, Protease

Enzyme and pathway databases

BioCyciBSUB:BSU23310-MONOMER
BRENDAi3.4.21.89 658

Protein family/group databases

MEROPSiS26.003

Names & Taxonomyi

Protein namesi
Recommended name:
Signal peptidase I S (EC:3.4.21.89)
Short name:
SPase I
Alternative name(s):
Leader peptidase I
Gene namesi
Name:sipS
Ordered Locus Names:BSU23310
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 18CytoplasmicSequence analysisAdd BLAST18
Transmembranei19 – 39HelicalSequence analysisAdd BLAST21
Topological domaini40 – 184ExtracellularSequence analysisAdd BLAST145

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi42D → S: No effect. 1 Publication1
Mutagenesisi43S → A or V: Loss of activity. 1 Publication1
Mutagenesisi43S → C or T: Reduced activity. 1 Publication1
Mutagenesisi44M → A: Increased activity. 1 Publication1
Mutagenesisi46P → A: Slightly reduced activity. 1 Publication1
Mutagenesisi47T → A: No effect. 1 Publication1
Mutagenesisi48L → A: Reduced activity. 1 Publication1
Mutagenesisi69G → A: Slightly reduced activity. 1 Publication1
Mutagenesisi70D → A: Slightly reduced activity. 1 Publication1
Mutagenesisi71I → A: Slightly reduced activity. 1 Publication1
Mutagenesisi72V → A: No effect. 1 Publication1
Mutagenesisi74L → A: Reduced activity. 1 Publication1
Mutagenesisi79V → A: No effect. 1 Publication1
Mutagenesisi81Y → A: Reduced activity. 1 Publication1
Mutagenesisi81Y → F: No effect. 1 Publication1
Mutagenesisi83K → A, H or R: Loss of activity. 1 Publication1
Mutagenesisi84R → A: Loss of activity. 1 Publication1
Mutagenesisi84R → H: Strongly reduced activity. 1 Publication1
Mutagenesisi84R → K: No effect. 1 Publication1
Mutagenesisi86I → A: Slightly reduced activity. 1 Publication1
Mutagenesisi87G → A: No effect. 1 Publication1
Mutagenesisi88L → A: Reduced activity. 1 Publication1
Mutagenesisi89P → A: No effect. 1 Publication1
Mutagenesisi90G → A: No effect. 1 Publication1
Mutagenesisi91D → A, E or N: No effect. 1 Publication1
Mutagenesisi141Y → A: No effect. 1 Publication1
Mutagenesisi145G → A: Strongly reduced activity. 1 Publication1
Mutagenesisi146D → A or N: Strongly reduced activity. 1 Publication1
Mutagenesisi146D → E: No effect. 1 Publication1
Mutagenesisi147N → A: Reduced activity. 1 Publication1
Mutagenesisi150N → A: No effect. 1 Publication1
Mutagenesisi151S → A: Reduced activity. 1 Publication1
Mutagenesisi153D → A: Strongly reduced activity. 1 Publication1
Mutagenesisi153D → E or N: Loss of activity. 1 Publication1
Mutagenesisi154S → A: Slightly reduced activity. 1 Publication1
Mutagenesisi155R → A: Reduced activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001094991 – 184Signal peptidase I SAdd BLAST184

Proteomic databases

PaxDbiP28628

Expressioni

Inductioni

Expressed at the postexponential growth phase; regulated by the DegS-DegU system.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100012791

Structurei

3D structure databases

ProteinModelPortaliP28628
SMRiP28628
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S26 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C3F Bacteria
COG0681 LUCA
HOGENOMiHOG000003673
InParanoidiP28628
KOiK03100
OMAiNDGRYFG
PhylomeDBiP28628

Family and domain databases

InterProiView protein in InterPro
IPR036286 LexA/Signal_pep-like_sf
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
IPR015927 Peptidase_S24_S26A/B/C
PfamiView protein in Pfam
PF00717 Peptidase_S24, 1 hit
PRINTSiPR00727 LEADERPTASE
SUPFAMiSSF51306 SSF51306, 1 hit
TIGRFAMsiTIGR02227 sigpep_I_bact, 1 hit
PROSITEiView protein in PROSITE
PS00501 SPASE_I_1, 1 hit
PS00760 SPASE_I_2, 1 hit
PS00761 SPASE_I_3, 1 hit

Sequencei

Sequence statusi: Complete.

P28628-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSENVSKKK SILEWAKAIV IAVVLALLIR NFIFAPYVVD GDSMYPTLHN
60 70 80 90 100
RERVFVNMTV KYIGEFDRGD IVVLNGDDVH YVKRIIGLPG DTVEMKNDQL
110 120 130 140 150
YINGKKVDEP YLAANKKRAK QDGFDHLTDD FGPVKVPDNK YFVMGDNRRN
160 170 180
SMDSRNGLGL FTKKQIAGTS KFVFYPFNEM RKTN
Length:184
Mass (Da):21,047
Last modified:December 1, 1992 - v1
Checksum:i5A2D005BF0D33CE9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11847 Genomic DNA Translation: CAA77871.1
L09228 Genomic DNA Translation: AAA67478.1
AL009126 Genomic DNA Translation: CAB14263.1
PIRiS23381
RefSeqiNP_390212.1, NC_000964.3
WP_003246166.1, NZ_JNCM01000036.1

Genome annotation databases

EnsemblBacteriaiCAB14263; CAB14263; BSU23310
GeneIDi938944
KEGGibsu:BSU23310
PATRICifig|224308.179.peg.2537

Similar proteinsi

Entry informationi

Entry nameiLEPS_BACSU
AccessioniPrimary (citable) accession number: P28628
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: March 28, 2018
This is version 139 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health