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UniProtKB/Swiss-Prot entry P00803


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

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Entry information
Entry name LEP_ECOLI
Primary accession number P00803
Secondary accession numbers P78098 Q2MAG2
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 89)
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: b2568, JW2552
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6311837 [NCBI, ExPASy, EBI, Israel, Japan]
Wolfe P.B., Wickner W., Goodman J.M.;
"Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope.";
J. Biol. Chem. 258:12073-12080(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
Nashimoto H., Saito N.;
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
TOPOLOGY.
PubMed=16453726 [NCBI, ExPASy, EBI, Israel, Japan]
von Heijne G.;
"The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology.";
EMBO J. 5:3021-3027(1986).
[6]
TOPOLOGY.
PubMed=2202591 [NCBI, ExPASy, EBI, Israel, Japan]
Bilgin N., Lee J.I., Zhu H.Y., Dalbey R., von Heijne G.;
"Mapping of catalytically important domains in Escherichia coli leader peptidase.";
EMBO J. 9:2717-2722(1990).
[7]
MUTAGENESIS, AND ACTIVE SITES.
PubMed=1618816 [NCBI, ExPASy, EBI, Israel, Japan]
Sung M., Dalbey R.E.;
"Identification of potential active-site residues in the Escherichia coli leader peptidase.";
J. Biol. Chem. 267:13154-13159(1992).
[8]
MUTAGENESIS.
STRAIN=HJM114, and IT41;
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).
[9]
MUTAGENESIS, AND ACTIVE SITES.
PubMed=8394311 [NCBI, ExPASy, EBI, Israel, Japan]
Black M.T.;
"Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad.";
J. Bacteriol. 175:4957-4961(1993).
[10]
TOPOLOGY.
PubMed=2551889 [NCBI, ExPASy, EBI, Israel, Japan]
San Millan J.L., Boyd D., Dalbey R., Wickner W., Beckwith J.;
"Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase.";
J. Bacteriol. 171:5536-5541(1989).
[11]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.1109730; PubMed=15919996 [NCBI, ExPASy, EBI, Israel, Japan]
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane proteome.";
Science 308:1321-1323(2005).
[12]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 77-324.
DOI=10.1038/24196; PubMed=9823901 [NCBI, ExPASy, EBI, Israel, Japan]
Paetzel M., Dalbey R.E., Strynadka N.C.;
"Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor.";
Nature 396:186-190(1998).
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
K00426; AAA24064.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D64044; BAA10915.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75621.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76744.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G65034; ZPECS.
RefSeq AP_003154.1; -.
NP_417063.1; -.
3D structure databases
PDB
1B12; X-ray; 1.95 A; A/B/C/D=77-324.[ExPASy / RCSB / EBI]
1KN9; X-ray; 2.40 A; A/B/C/D=77-324.[ExPASy / RCSB / EBI]
1T7D; X-ray; 2.47 A; A/B=76-324.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1B12; -.
1KN9; -.
1T7D; -.
ModBase P00803.
Protein-protein interaction databases
IntAct P00803; -.
Protein family/group databases
MEROPS S26.001; -.
Enzyme and pathway databases
BioCyc EcoCyc:EG10530-MON; -.
Organism-specific databases
EchoBASE EB0525; -.
EcoGene EG10530; lepB.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
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.
BLOCKS P00803.
ProtoNet P00803.
Genome annotation databases
GeneID 947040; -.
GenomeReviews U00096_GR; b2568.
AP009048_GR; JW2552.
KEGG ecj:JW2552; -.
eco:b2568; -.
Phylogenomic databases
HOGENOM P00803; -.
Genome annotation databases
CMR P00803; b2568.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; Membrane; Protease; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   324  324     Signal peptidase I. PRO_0000109506
TOPO_DOM   1     3  3     Periplasmic (Probable). 
TRANSMEM   4    22  19     Probable. 
TOPO_DOM   23    58  36     Cytoplasmic (Probable). 
TRANSMEM   59    77  19     Probable. 
TOPO_DOM   78   324  247     Periplasmic (Probable). 
ACT_SITE   91    91         
ACT_SITE   146   146         
MOD_RES   1     1        Blocked amino end (Met). 
DISULFID   171   177         
MUTAGEN   62    62        E->V: Indifferent. 
MUTAGEN   78    78        R->E,N,L: Indifferent. 
MUTAGEN   91    91        S->A: Loss of activity. 
MUTAGEN   125   125        H->N: Indifferent. 
MUTAGEN   128   128        R->Q: Small effect. 
MUTAGEN   130   130        D->A: Indifferent. 
MUTAGEN   144   144        Y->F: Indifferent. 
MUTAGEN   146   146        K->M,D,G,S: Loss of activity. 
MUTAGEN   147   147        R->Q: Small effect. 
MUTAGEN   154   154        D->A: Loss of activity. 
MUTAGEN   154   154        D->N: Indifferent. 
MUTAGEN   159   159        D->N: Small effect. 
MUTAGEN   171   171        C->A: Indifferent. 
MUTAGEN   177   177        C->A: Indifferent. 
MUTAGEN   236   236        H->N: Indifferent. 
MUTAGEN   269   269        Y->F: Indifferent. 
MUTAGEN   274   274        D->A: Indifferent. 
MUTAGEN   276   276        R->Q: Small effect. 
MUTAGEN   281   281        D->A: Indifferent. 
MUTAGEN   283   283        R->Q: Small effect. 
CONFLICT   42    43        AG -> R (in Ref. 1 and 2). 
CONFLICT   123   123        T -> N (in Ref. 1 and 2). 
CONFLICT   183   183        V -> A (in Ref. 1 and 2). 
STRAND   82    86  5      
TURN   91    95  5      
STRAND   100   112  13      
HELIX   114   116  3      
STRAND   119   123  5      
STRAND   131   135  5      
STRAND   142   150  9      
STRAND   155   159  5      
TURN   160   163  4      
STRAND   164   168  5      
STRAND   183   185  3      
STRAND   189   198  10      
HELIX   200   202  3      
STRAND   205   211  7      
STRAND   221   231  11      
STRAND   234   240  7      
HELIX   248   250  3      
STRAND   261   263  3      
STRAND   268   272  5      
HELIX   282   285  4      
HELIX   290   292  3      
STRAND   293   304  12      
HELIX   317   319  3      
Sequence information
Length: 324 AA [This is the length of the unprocessed precursor] Molecular weight: 35960 Da [This is the MW of the unprocessed precursor] CRC64: 9419710D7212E660 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MANMFALILV IATLVTGILW CVDKFFFAPK RRERQAAAQA AAGDSLDKAT LKKVAPKPGW 

        70         80         90        100        110        120 
LETGASVFPV LAIVLIVRSF IYEPFQIPSG SMMPTLLIGD FILVEKFAYG IKDPIYQKTL 

       130        140        150        160        170        180 
IETGHPKRGD IVVFKYPEDP KLDYIKRAVG LPGDKVTYDP VSKELTIQPG CSSGQACENA 

       190        200        210        220        230        240 
LPVTYSNVEP SDFVQTFSRR NGGEATSGFF EVPKNETKEN GIRLSERKET LGDVTHRILT 

       250        260        270        280        290        300 
VPIAQDQVGM YYQQPGQQLA TWIVPPGQYF MMGDNRDNSA DSRYWGFVPE ANLVGRATAI 

       310        320 
WMSFDKQEGE WPTGLRLSRI GGIH 

P00803 in FASTA format

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