LSPA_HELPY
ID LSPA_HELPY Reviewed; 157 AA.
AC P25178;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 135.
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}; Synonyms=ureD;
GN OrderedLocusNames=HP_0074;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=85P;
RX PubMed=2001995; DOI=10.1128/jb.173.6.1920-1931.1991;
RA Labigne A., Cussac V., Courcoux P.;
RT "Shuttle cloning and nucleotide sequences of Helicobacter pylori genes
RT responsible for urease activity.";
RL J. Bacteriol. 173:1920-1931(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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, ECO:0000305}.
CC -!- CAUTION: Was originally thought to be related to urease function.
CC {ECO:0000305|PubMed:2001995}.
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DR EMBL; M60398; AAA25019.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07145.1; -; Genomic_DNA.
DR PIR; B64529; B64529.
DR RefSeq; NP_206874.1; NC_000915.1.
DR RefSeq; WP_000921378.1; NC_018939.1.
DR AlphaFoldDB; P25178; -.
DR SMR; P25178; -.
DR IntAct; P25178; 3.
DR STRING; 85962.C694_00360; -.
DR PaxDb; P25178; -.
DR EnsemblBacteria; AAD07145; AAD07145; HP_0074.
DR KEGG; hpy:HP_0074; -.
DR PATRIC; fig|85962.47.peg.78; -.
DR eggNOG; COG0597; Bacteria.
DR OMA; IEFGMVF; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000000429; 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..157
FT /note="Lipoprotein signal peptidase"
FT /id="PRO_0000178784"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 114
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 131
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT CONFLICT 13
FT /note="M -> I (in Ref. 1; AAA25019)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="M -> V (in Ref. 1; AAA25019)"
FT /evidence="ECO:0000305"
FT CONFLICT 124..157
FT /note="FAIFNFADVMIDVGVGVLLLKQFFFKQKQNKIKA -> LPFLTSLMS (in
FT Ref. 1; AAA25019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 157 AA; 17998 MW; 738CF045ED01006C CRC64;
MLKTTKKSLL VFMGVFFLIF GVDQAIKYAI LEGFRYESLM IDIVLVFNKG VAFSLLSFLE
GGLKYLQILL ILGLFIFLMR QRELFKNHAI EFGMVFGAGV SNVLDRFVHG GVVDYVYYHY
GFDFAIFNFA DVMIDVGVGV LLLKQFFFKQ KQNKIKA
