(data stored in ACNUC7421 zone)

SWISSPROT: Q2ILW1_ANADE

ID   Q2ILW1_ANADE            Unreviewed;       206 AA.
AC   Q2ILW1;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 92.
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=Adeh_0013 {ECO:0000313|EMBL:ABC79791.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79791.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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:SAAS01181907}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of signal peptides from bacterial membrane
CC         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.; EC=3.4.23.36; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00161, ECO:0000256|RuleBase:RU000594,
CC         ECO:0000256|SAAS:SAAS01181912};
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal
CC       peptide cleavage). {ECO:0000256|HAMAP-Rule:MF_00161,
CC       ECO:0000256|SAAS:SAAS01181909}.
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:SAAS01181910}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00161}.
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DR   EMBL; CP000251; ABC79791.1; -; Genomic_DNA.
DR   RefSeq; WP_011419074.1; NC_007760.1.
DR   STRING; 290397.Adeh_0013; -.
DR   MEROPS; A08.001; -.
DR   EnsemblBacteria; ABC79791; ABC79791; Adeh_0013.
DR   KEGG; ade:Adeh_0013; -.
DR   eggNOG; ENOG4107TEJ; Bacteria.
DR   eggNOG; COG0597; LUCA.
DR   HOGENOM; HOG000096992; -.
DR   KO; K03101; -.
DR   OMA; FIEDYWH; -.
DR   BioCyc; ADEH290397:G1G5W-14-MONOMER; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000001935; 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-UniRule.
DR   HAMAP; MF_00161; LspA; 1.
DR   InterPro; IPR001872; Peptidase_A8.
DR   PANTHER; PTHR33695; PTHR33695; 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; Q2ILW1.
DR   SWISS-2DPAGE; Q2ILW1.
KW   Aspartyl protease {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS01181908};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS01181901};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS01181933,
KW   ECO:0000313|EMBL:ABC79791.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS01181906};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|RuleBase:RU000594, ECO:0000256|SAAS:SAAS01181905};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS01181903};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161,
KW   ECO:0000256|SAAS:SAAS01181900}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    206       Lipoprotein signal peptidase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004210527.
FT   TRANSMEM     94    115       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   TRANSMEM    127    145       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   TRANSMEM    165    184       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00161}.
FT   ACT_SITE    142    142       {ECO:0000256|HAMAP-Rule:MF_00161}.
FT   ACT_SITE    172    172       {ECO:0000256|HAMAP-Rule:MF_00161}.
SQ   SEQUENCE   206 AA;  24054 MW;  B11E54E58B979D36 CRC64;
     MRRPVSKWAL LALLFTALLA ADQWTKYLAV ERLTVVFERG GDETLAERVR GFYTYRHLEP
     LSTEPYYVWR PVWRMNYVEN PGAAWGLFRG HSQFFRNAFF TLVSVAAVAF ILHYYRKLRQ
     DQRYLQVALG LVLAGAVGNF VDRLARRYVI DFIEWYWWNR PDIRWPTFNV ADSLIVVGVA
     MLVLHPGSRR EAARAPARRD AAAERV
//

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