ID   LSPA_FUSNN              Reviewed;         165 AA.
AC   Q8RH46;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Lipoprotein signal peptidase {ECO:0000255|HAMAP-Rule:MF_00161};
DE            EC=3.4.23.36 {ECO:0000255|HAMAP-Rule:MF_00161};
DE   AltName: Full=Prolipoprotein signal peptidase {ECO:0000255|HAMAP-Rule:MF_00161};
DE   AltName: Full=Signal peptidase II {ECO:0000255|HAMAP-Rule:MF_00161};
DE            Short=SPase II {ECO:0000255|HAMAP-Rule:MF_00161};
GN   Name=lspA {ECO:0000255|HAMAP-Rule:MF_00161}; OrderedLocusNames=FN0068;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
CC   -!- FUNCTION: This protein specifically catalyzes the removal of signal
CC       peptides from prolipoproteins. {ECO:0000255|HAMAP-Rule:MF_00161}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of signal peptides from bacterial membrane
CC         prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in
CC         which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and
CC         Zaa (Gly or Ala) have small, neutral side chains.; EC=3.4.23.36;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00161};
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal peptide
CC       cleavage). {ECO:0000255|HAMAP-Rule:MF_00161}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00161}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00161}.
CC   -!- SIMILARITY: Belongs to the peptidase A8 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00161}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009951; AAL94281.1; -; Genomic_DNA.
DR   RefSeq; NP_602982.1; NC_003454.1.
DR   AlphaFoldDB; Q8RH46; -.
DR   SMR; Q8RH46; -.
DR   STRING; 190304.FN0068; -.
DR   EnsemblBacteria; AAL94281; AAL94281; FN0068.
DR   KEGG; fnu:FN0068; -.
DR   PATRIC; fig|190304.8.peg.660; -.
DR   eggNOG; COG0597; Bacteria.
DR   HOGENOM; CLU_083252_3_3_0; -.
DR   InParanoid; Q8RH46; -.
DR   OMA; WKFKLIV; -.
DR   BioCyc; FNUC190304:G1FZS-681-MON; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000002521; 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   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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;
KW   Aspartyl protease; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW   Protease; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..165
FT                   /note="Lipoprotein signal peptidase"
FT                   /id="PRO_0000289384"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   165 AA;  18976 MW;  BD2F9455511F1F16 CRC64;
     MSKMCSSVEI GDSMIYIFLF LILLIIDQYS KFIVDSTLSV GETVPVIDGF FNLTYVQNRG
     VAFGLFQGKI DIVSILAVIA IGLILFYFCK NFKKISFLER IAYTMIFSGA IGNMIDRLFR
     AYVVDMLDFR GIWSFIFNFA DVWINIGVVL IIVEHIFFNR KKRVK