Reviewed, UniProtKB/Swiss-Prot P26844 (LEP_PSEFL)

Names and origin

Protein names

Recommended name:
    Signal peptidase I
      Short name=SPase I
    EC=3.4.21.89
Alternative name(s):
    Leader peptidase I

Gene names

Name:

lepB

Organism

Pseudomonas fluorescens

Taxonomic identifier

294 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	284 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
Subcellular location	Cell inner membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the peptidase S26 family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane
Molecular function	Hydrolase Protease
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred 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 – 284	284	Signal peptidase I		PRO_0000109514
Regions
	Transmembrane	4 – 22	19	Potential
	Topological domain	23 – 58	36	Cytoplasmic Potential
	Transmembrane	59 – 77	19	Potential
	Topological domain	78 – 284	207	Periplasmic Potential
Sites
	Active site	90	1	By similarity
	Active site	145	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P26844-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: B1B89D956BDA7891	FASTA	284	31,903
	10 20 30 40 50 60 MSLNFPLLLV IAVAVCGLLA LLDLVFFAPR RRSAIASYQG SVSQPDAVVI EKLNKEPLLV 70 80 90 100 110 120 EYGKSFFPVL FIVLVLRSFL VEPFQIPSGS MKPTLDVGDF ILVNKFSYGI RLPVIDKKVI 130 140 150 160 170 180 EVGDPQRGDV MVFRYPSDPN VNYIKRVVGL PGDVVRYTSD KRLFINGESV AEKLLGAEPN 190 200 210 220 230 240 TLGSAELYQE KLGAVEHEIR KEMSRYRAMP DGQWKVPAGH YFMMGDNRDN SNDSRYWDDP 250 260 270 280 NIPKDLLGMV PDENIVGKAF AVWMSWPEPK LSHLPNFSRV GLIK

References

[1]	"On the catalytic mechanism of prokaryotic leader peptidase 1." Black M.T., Munn J.G.R., Allsop A.E. Biochem. J. 282:539-543(1992) [PubMed: 1546969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 49323 / NCIMB 10586.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X56466 Genomic DNA. Translation: CAA39839.1.
PIR	S22414.
3D structure databases
HSSP	HSSP built from PDB template 1KN9 based on UniProtKB P00803.
ModBase	Search...
Protein family/group databases
MEROPS	S26.001.
Enzyme and pathway databases
BRENDA	3.4.21.89. 329.
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_cons-reg. IPR011056. Peptidase_S24_S26A/B/C_b-rbn. [Graphical view]
Gene3D	G3DSA:2.10.109.10. Pept_S24_S26_C. 1 hit.
Pfam	PF00717. Peptidase_S24. 1 hit. [Graphical view]
PRINTS	PR00727. LEADERPTASE.
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

LEP_PSEFL

Accession

Primary (citable) accession number: P26844

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)