(data stored in SCRATCH zone)

SWISSPROT: C6AYD9_RHILS

ID   C6AYD9_RHILS            Unreviewed;       167 AA.
AC   C6AYD9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 62.
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=Rleg_0052 {ECO:0000313|EMBL:ACS54363.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54363.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54363.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54363.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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; CP001622; ACS54363.1; -; Genomic_DNA.
DR   RefSeq; WP_012755795.1; NC_012850.1.
DR   EnsemblBacteria; ACS54363; ACS54363; Rleg_0052.
DR   KEGG; rlg:Rleg_0052; -.
DR   HOGENOM; HOG000096993; -.
DR   KO; K03101; -.
DR   OMA; GFDFAIF; -.
DR   OrthoDB; POG091H059F; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000002256; 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; C6AYD9.
DR   SWISS-2DPAGE; C6AYD9.
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:UP000002256};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS00112525};
KW   Lipoprotein {ECO:0000313|EMBL:ACS54363.1};
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   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     18     36       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   TRANSMEM     48     67       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   TRANSMEM     73     91       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   TRANSMEM     98    116       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   TRANSMEM    136    161       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   ACT_SITE    117    117       {ECO:0000256|HAMAP-Rule:MF_00161}.
FT   ACT_SITE    144    144       {ECO:0000256|HAMAP-Rule:MF_00161}.
SQ   SEQUENCE   167 AA;  18768 MW;  0C2D9AFC69273F1F CRC64;
     MTEQTHARPA LFSRPAPILF FIVVAVLIDQ AVKIAVDHYL PLQEAVPVVP MLALYRTYNL
     GVAFSMLSGM DGWFIVGMRL IIVAFVIWLW YRTAKDRWIA HLGYALIIAG AIGNLVDRFA
     YGHVIDYILF YTESWSFAVF NLADSFITIG AGCVILDELL LPKKASR
//

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