LSPA_CHLTA
ID LSPA_CHLTA Reviewed; 167 AA.
AC Q3KLU5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=CTA_0443;
OS Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=315277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT genitotropic strains.";
RL Infect. Immun. 73:6407-6418(2005).
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; CP000051; AAX50677.1; -; Genomic_DNA.
DR RefSeq; WP_009871760.1; NC_007429.1.
DR AlphaFoldDB; Q3KLU5; -.
DR SMR; Q3KLU5; -.
DR EnsemblBacteria; AAX50677; AAX50677; CTA_0443.
DR KEGG; cta:CTA_0443; -.
DR HOGENOM; CLU_083252_3_0_0; -.
DR OMA; IEFGMVF; -.
DR UniPathway; UPA00665; -.
DR Proteomes; UP000002532; 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; Transmembrane; Transmembrane helix.
FT CHAIN 1..167
FT /note="Lipoprotein signal peptidase"
FT /id="PRO_0000289362"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 46..66
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 101..121
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
FT TRANSMEM 139..159
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 143
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00161"
SQ SEQUENCE 167 AA; 18940 MW; 0B9752F830B01F12 CRC64;
MPTRSLPTFL TLLLLASIDW VSKLVVLLKS CQLSPHSSAF LYSYVWGHFS FLIIPSFNEG
AAFGLFTQYK IPLLIFRVCV ILGLALFLRI KYKSLHRRTR VALTLILAGA LGNVGDILLY
GKVVDFLSLS YYSWRFPSFN LADAFISIGT LLLIGHLYFT KESKKYF
