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Database: UniProt
Entry: C5ZYZ1_9HELI
LinkDB: C5ZYZ1_9HELI
Original site: C5ZYZ1_9HELI 
ID   C5ZYZ1_9HELI            Unreviewed;       148 AA.
AC   C5ZYZ1;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 71.
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   ECO:0000313|EMBL:EES89249.1};
GN   ORFNames=HCAN_0532 {ECO:0000313|EMBL:EES89249.1};
OS   Helicobacter canadensis MIT 98-5491.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=537970 {ECO:0000313|EMBL:EES89249.1, ECO:0000313|Proteomes:UP000007032};
RN   [1] {ECO:0000313|EMBL:EES89249.1, ECO:0000313|Proteomes:UP000007032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13241 {ECO:0000313|Proteomes:UP000007032};
RX   PubMed=19542273; DOI=10.1128/JB.00729-09;
RA   Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J.,
RA   Weinstock G.M., Wren B.W., Pallen M.J.;
RT   "Genome sequence of the emerging pathogen Helicobacter canadensis.";
RL   J. Bacteriol. 191:5566-5567(2009).
CC   -!- FUNCTION: This protein specifically catalyzes the removal of signal
CC       peptides from prolipoproteins. {ECO:0000256|HAMAP-Rule:MF_00161,
CC       ECO:0000256|RuleBase:RU000594}.
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:0000256|HAMAP-Rule:MF_00161,
CC         ECO:0000256|RuleBase:RU000594};
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal peptide
CC       cleavage). {ECO:0000256|HAMAP-Rule:MF_00161}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00161};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00161}.
CC   -!- SIMILARITY: Belongs to the peptidase A8 family.
CC       {ECO:0000256|ARBA:ARBA00006139, ECO:0000256|HAMAP-Rule:MF_00161,
CC       ECO:0000256|RuleBase:RU004181}.
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DR   EMBL; CM000776; EES89249.1; -; Genomic_DNA.
DR   RefSeq; WP_006655227.1; NZ_DS990368.1.
DR   AlphaFoldDB; C5ZYZ1; -.
DR   STRING; 537970.HCAN_0532; -.
DR   eggNOG; COG0597; Bacteria.
DR   HOGENOM; CLU_083252_4_3_7; -.
DR   OrthoDB; 9810259at2; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000007032; Chromosome.
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   NCBIfam; TIGR00077; lspA; 1.
DR   PANTHER; PTHR33695; LIPOPROTEIN SIGNAL PEPTIDASE; 1.
DR   PANTHER; PTHR33695:SF1; LIPOPROTEIN SIGNAL PEPTIDASE; 1.
DR   Pfam; PF01252; Peptidase_A8; 1.
DR   PRINTS; PR00781; LIPOSIGPTASE.
DR   PROSITE; PS00855; SPASE_II; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750, ECO:0000256|HAMAP-
KW   Rule:MF_00161};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00161};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00161};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00161, ECO:0000256|RuleBase:RU000594};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007032};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00161};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00161}.
FT   ACT_SITE        112
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00161"
SQ   SEQUENCE   148 AA;  17540 MW;  2E6C0EEAEC726816 CRC64;
     MPKQSLVSFF LALFLVLLID QAIKWWFVQS NFEYQGSVIS LVLVYNQGVA FSLFDFLKEW
     LKYLQILLLI GIFIYLWKHK EIFKTYSLPI GIIFGGGISN ILDRFLHIGV VDYIYWHYKF
     EFAIFNFADM MINLGVFLII LQTLFKKK
//
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