[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 49323 / NCIMB 10586; PubMed=1546969 [NCBI, ExPASy, EBI, Israel, Japan] Black M.T., Munn J.G.R., Allsop A.E.; "On the catalytic mechanism of prokaryotic leader peptidase 1."; Biochem. J. 282:539-543(1992).

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.
SIMILARITY: Belongs to the peptidase S26 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X56466; CAA39839.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S22414; S22414.

3D structure databases

HSSP

P00803; 1KN9. [HSSP ENTRY / PDB]

ModBase

P26844.

Protein family/group databases

MEROPS

S26.001; -.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0008236;	Molecular function: serine-type peptidase activity (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000223; Pept_S26A_signal_pept_1.
IPR011056; Peptidase_S24_S26_C.
IPR014037; Peptidase_S26A.
Graphical view of domain structure.

Gene3D

G3DSA:2.10.109.10; Pept_S24_S26_C; 1.

PANTHER

PTHR12383:SF1; Pept_S26A_signal_pept_1; 1.
PTHR12383; Peptidase_S26A; 1.

Pfam

PF00717; Peptidase_S24; 1.
Pfam graphical view of domain structure.

PRINTS

PR00727; LEADERPTASE.

TIGRFAMs

TIGR02227; sigpep_I_bact; 1.

PROSITE

PS00501; SPASE_I_1; 1.
PS00760; SPASE_I_2; 1.
PS00761; SPASE_I_3; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell inner membrane; Cell membrane; Hydrolase; Membrane; Protease; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 284`	`284`	`Signal peptidase I.`	`PRO_0000109514`
`TRANSMEM`	`4 22`	`19`	`Potential.`
`TOPO_DOM`	`23 58`	`36`	`Cytoplasmic (Potential).`
`TRANSMEM`	`59 77`	`19`	`Potential.`
`TOPO_DOM`	`78 284`	`207`	`Periplasmic (Potential).`
`ACT_SITE`	`90 90`		`By similarity.`
`ACT_SITE`	`145 145`		`By similarity.`

Sequence information

Length: 284 AA [This is the length of the unprocessed precursor]

Molecular weight: 31903 Da [This is the MW of the unprocessed precursor]

CRC64: B1B89D956BDA7891 [This is a checksum on the sequence]

        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

P26844 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools