(data stored in ACNUC7421 zone)

SWISSPROT: C5B7M5_EDWI9

ID   C5B7M5_EDWI9            Unreviewed;       166 AA.
AC   C5B7M5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 59.
DE   RecName: Full=Lipoprotein signal peptidase {ECO:0000256|HAMAP-Rule:MF_00161};
DE            EC=3.4.23.36 {ECO:0000256|HAMAP-Rule:MF_00161};
DE   AltName: Full=Prolipoprotein signal peptidase {ECO:0000256|HAMAP-Rule:MF_00161};
DE   AltName: Full=Signal peptidase II {ECO:0000256|HAMAP-Rule:MF_00161};
DE            Short=SPase II {ECO:0000256|HAMAP-Rule:MF_00161};
GN   Name=lspA {ECO:0000256|HAMAP-Rule:MF_00161};
GN   OrderedLocusNames=NT01EI_0680 {ECO:0000313|EMBL:ACR67902.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67902.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein specifically catalyzes the removal of
CC       signal peptides from prolipoproteins. {ECO:0000256|HAMAP-
CC       Rule:MF_00161, ECO:0000256|RuleBase:RU000594,
CC       ECO:0000256|SAAS:SAAS00395969}.
CC   -!- CATALYTIC ACTIVITY: Release of signal peptides from bacterial
CC       membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-
CC       (S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably
CC       Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small,
CC       neutral side chains. {ECO:0000256|HAMAP-Rule:MF_00161,
CC       ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS00396003}.
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal
CC       peptide cleavage). {ECO:0000256|HAMAP-Rule:MF_00161,
CC       ECO:0000256|SAAS:SAAS00396035}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00161}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00161}.
CC   -!- SIMILARITY: Belongs to the peptidase A8 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00161, ECO:0000256|RuleBase:RU004181,
CC       ECO:0000256|SAAS:SAAS00581686}.
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DR   EMBL; CP001600; ACR67902.1; -; Genomic_DNA.
DR   STRING; 634503.NT01EI_0680; -.
DR   MEROPS; A08.001; -.
DR   EnsemblBacteria; ACR67902; ACR67902; NT01EI_0680.
DR   KEGG; eic:NT01EI_0680; -.
DR   eggNOG; ENOG4105M02; Bacteria.
DR   eggNOG; COG0597; LUCA.
DR   HOGENOM; HOG000096993; -.
DR   KO; K03101; -.
DR   OMA; NRWYFPA; -.
DR   OrthoDB; POG091H059F; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00161; LspA; 1.
DR   InterPro; IPR001872; Peptidase_A8.
DR   PANTHER; PTHR33695:SF2; PTHR33695:SF2; 1.
DR   Pfam; PF01252; Peptidase_A8; 1.
DR   PRINTS; PR00781; LIPOSIGPTASE.
DR   TIGRFAMs; TIGR00077; lspA; 1.
DR   PROSITE; PS00855; SPASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B7M5.
DR   SWISS-2DPAGE; C5B7M5.
KW   Aspartyl protease {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS00112503};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS00112556};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS00112525,
KW   ECO:0000313|EMBL:ACR67902.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS00112491};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS00112585};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS00112497};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS00112465}.
FT   TRANSMEM     12     32       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   TRANSMEM     71     88       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   TRANSMEM    100    118       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   TRANSMEM    138    158       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   ACT_SITE    115    115       {ECO:0000256|HAMAP-Rule:MF_00161}.
FT   ACT_SITE    142    142       {ECO:0000256|HAMAP-Rule:MF_00161}.
SQ   SEQUENCE   166 AA;  18618 MW;  EF5A3DC387635408 CRC64;
     MMRRPIFSTG LRWLWIVVAV LIVDLGSKQL ILQHFMLGET LPLFPSLNLH YARNYGAAFS
     FLADSGGWQR WFFAGIAIAI CVALLVMMYR SAASQRLSNI AYALIIGGAL GNLFDRLWHG
     FVVDMIDFYV GNWHFATFNL ADTAICIGAA LVVVEGFLPQ RDKENK
//

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