ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8L2J7

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name LEP_RICTY
Primary accession number Q8L2J7
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 45)
Name and origin of the protein
Protein name Signal peptidase I
Synonyms SPase I
EC 3.4.21.89
Leader peptidase I
Gene name
Name: lepB
OrderedLocusNames: RT0020
From
Rickettsia typhi [TaxID: 785] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION IN E.COLI.
STRAIN=Ethiopian AZ322;
DOI=10.1128/JB.185.15.4578-4584.2003; PubMed=12867468 [NCBI, ExPASy, EBI, Israel, Japan]
Rahman M.S., Simser J.A., Macaluso K.R., Azad A.F.;
"Molecular and functional analysis of the lepB gene, encoding a type I signal peptidase from Rickettsia rickettsii and Rickettsia typhi.";
J. Bacteriol. 185:4578-4584(2003).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC VR-144 / Wilmington;
DOI=10.1128/JB.186.17.5842-5855.2004; PubMed=15317790 [NCBI, ExPASy, EBI, Israel, Japan]
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C., Yu X.-J., Walker D.H., Weinstock G.M.;
"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae.";
J. Bacteriol. 186:5842-5855(2004).
Comments
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
AF503336; AAM22228.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017197; AAU03508.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_066990.1; -.
3D structure databases
HSSP P00803; 1B12. [HSSP ENTRY / PDB]
ModBase Q8L2J7.
Protein family/group databases
MEROPS S26.001; -.
Enzyme and pathway databases
BioCyc RTYP257363:RT0020-MON; -.
Ontologies
GO
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 PS00760; SPASE_I_2; 1.
PS00761; SPASE_I_3; 1.
Genome annotation databases
GeneID 2958484; -.
GenomeReviews AE017197_GR; RT0020.
KEGG rty:RT0020; -.
Phylogenomic databases
HOGENOM Q8L2J7; -.
Genome annotation databases
CMR Q8L2J7; RT0020.
Other
ProtoNet Q8L2J7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; Membrane; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   264  264     Signal peptidase I. PRO_0000316278
TOPO_DOM   1    18  18     Cytoplasmic (Potential). 
TRANSMEM   19    39  21     Potential. 
TOPO_DOM   40   264  225     Periplasmic (Potential). 
ACT_SITE   43    43        By similarity. 
ACT_SITE   106   106        By similarity. 
Sequence information
Length: 264 AA [This is the length of the unprocessed precursor] Molecular weight: 30849 Da [This is the MW of the unprocessed precursor] CRC64: E35E28BD4585A002 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNRDNTKTNK TVKQEFASFT FVICIALVIR ILIMEPFTVP TGSMKATILE NDYIFSTKYS 

        70         80         90        100        110        120 
YGYSNYSLSF FDFIPLFKGR VFAREPERGD IVVFRPPNDM SVRYIKRLIG LPGDKIQLID 

       130        140        150        160        170        180 
DVIYINDKKI ERTEVGTYIG EDGIKYLKFK ETLPNGRTYF SYKLAPIFGI ISNDRYSNTG 

       190        200        210        220        230        240 
VFYVPEGQYF FLGDNRDRSN DSRVNLGFVP FENFIGKAQF IWFSTKITWW DNDIGIINLI 

       250        260 
LKLKPWIESV RLSRIFKNLY NVDE
Q8L2J7 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!