LSPA_HAES1
ID LSPA_HAES1 Reviewed; 165 AA.
AC Q0I1V9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=HS_0185;
OS Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=205914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129Pt;
RX PubMed=17172329; DOI=10.1128/jb.01422-06;
RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA Xie G., Inzana T.J.;
RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT influenzae Rd.";
RL J. Bacteriol. 189:1890-1898(2007).
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}.
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DR EMBL; CP000436; ABI24463.1; -; Genomic_DNA.
DR RefSeq; WP_011608338.1; NC_008309.1.
DR AlphaFoldDB; Q0I1V9; -.
DR SMR; Q0I1V9; -.
DR STRING; 205914.HS_0185; -.
DR EnsemblBacteria; ABI24463; ABI24463; HS_0185.
DR KEGG; hso:HS_0185; -.
DR eggNOG; COG0597; Bacteria.
DR HOGENOM; CLU_083252_4_0_6; -.
DR OMA; NRWYFPA; -.
DR UniPathway; UPA00665; -.
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.
PE 3: Inferred from homology;
KW Aspartyl protease; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..165
FT /note="Lipoprotein signal peptidase"
FT /id="PRO_0000289389"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 97..119
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 121
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT ACT_SITE 139
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ SEQUENCE 165 AA; 18778 MW; E4DEE038F0A726BA CRC64;
MNLSKTGLPF LWISAVAFFT DLITKLAVVK NFSLYESINI LPFFNLTYVR NHGAAFSFLA
DHAGWQKYFF ILLALVVSFM ILFFLYKNQA TQKLQNTGYA LMVGGALANA ADRAYHGFVV
DFFDFYWQQW HYPVFNIADV AICIGAGLLA IDAFKQNDKK ESKQN
