NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0140-6736(02)08713-5; PubMed=12044378 [NCBI, ExPASy, EBI, Israel, Japan]
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
"Genome and virulence determinants of high virulence community-acquired MRSA.";
Lancet 359:1819-1827(2002).

Comments

FUNCTION: Essential for cell viability (By similarity).
CATALYTIC ACTIVITY: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein (Potential).
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

BA000033; BAB94712.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_645664.1; -.

3D structure databases

HSSP

P00803; 1B12. [HSSP ENTRY / PDB]

ModBase

P0A069.

Protein family/group databases

MEROPS

S26.016; -.

Enzyme and pathway databases

BioCyc

SAUR196620:MW0847-MON; -.

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.

Genome annotation databases

GeneID

1002959; -.

GenomeReviews

BA000033_GR; MW0847.

KEGG

sam:MW0847; -.

Phylogenomic databases

HOGENOM

P0A069; -.

Genome annotation databases

CMR

P0A069; MW0847.

Other

ProtoNet

P0A069.

UniRef

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

Keywords

Cell membrane; Complete proteome; Hydrolase; Membrane; Protease; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 191`	`191`	`Signal peptidase IB.`	`PRO_0000109531`
`TOPO_DOM`	`1 7`	`7`	`Cytoplasmic (Potential).`
`TRANSMEM`	`8 28`	`21`	`Potential.`
`TOPO_DOM`	`29 191`	`163`	`Extracellular (Potential).`
`ACT_SITE`	`36 36`		`By similarity.`
`ACT_SITE`	`77 77`		`By similarity.`

Sequence information

Length: 191 AA [This is the length of the unprocessed precursor]

Molecular weight: 21692 Da [This is the MW of the unprocessed precursor]

CRC64: 1C6BF5BB423706C0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKELLEWII SIAVAFVILF IVGKFIVTPY TIKGESMDPT LKDGERVAVN IIGYKTGGLE 

        70         80         90        100        110        120 
KGNVVVFHAN KNDDYVKRVI GVPGDKVEYK NDTLYVNGKK QDEPYLNYNL KHKQGDYITG 

       130        140        150        160        170        180 
TFQVKDLPNA NPKSNVIPKG KYLVLGDNRE VSKDSRAFGL IDEDQIVGKV SFRFWPFSEF 

       190 
KHNFNPENTK N

P0A069 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