ID   L1137_LEGPH             Reviewed;         322 AA.
AC   Q5ZWE8;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Serine protease Lpg1137 {ECO:0000305};
DE            EC=3.4.22.- {ECO:0000269|PubMed:28504273};
GN   OrderedLocusNames=lpg1137 {ECO:0000312|EMBL:AAU27223.1};
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(2004).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, ACTIVE SITE, AND MUTAGENESIS OF SER-68 AND
RP   SER-134.
RX   PubMed=28504273; DOI=10.1038/ncomms15406;
RA   Arasaki K., Mikami Y., Shames S.R., Inoue H., Wakana Y., Tagaya M.;
RT   "Legionella effector Lpg1137 shuts down ER-mitochondria communication
RT   through cleavage of syntaxin 17.";
RL   Nat. Commun. 8:15406-15406(2017).
RN   [3]
RP   CAUTION.
RX   PubMed=28966893; DOI=10.7717/peerj.3849;
RA   Gradowski M., Pawlowski K.;
RT   "The Legionella pneumophila effector Lpg1137 is a homologue of
RT   mitochondrial SLC25 carrier proteins, not of known serine proteases.";
RL   PeerJ 5:e3849-e3849(2017).
CC   -!- FUNCTION: Serine protease effector that inhibits host cell autophagy by
CC       targeting SNX17 (PubMed:28504273). Localizes to the host endoplasmic
CC       reticulum-mitochondria contact site and catalyzes degradation of host
CC       SNX17, thereby impairing endoplasmic reticulum-mitochondria
CC       communication, leading to inhibit autophagy as well as staurosporine-
CC       induced apoptosis (PubMed:28504273). {ECO:0000269|PubMed:28504273}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28504273}. Host
CC       mitochondrion membrane {ECO:0000269|PubMed:28504273}. Note=Localizes to
CC       the host mitochondria-associated endoplasmic reticulum membrane (MAM).
CC       {ECO:0000269|PubMed:28504273}.
CC   -!- CAUTION: According to a report based on bioinformatics studies, this
CC       protein is not related to serine proteases but is homologous to
CC       mitochondrial SLC25 carrier proteins. Additional experimental evidences
CC       are needed to confirm this prediction. {ECO:0000305|PubMed:28966893}.
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DR   EMBL; AE017354; AAU27223.1; -; Genomic_DNA.
DR   RefSeq; WP_010946871.1; NC_002942.5.
DR   RefSeq; YP_095170.1; NC_002942.5.
DR   STRING; 272624.lpg1137; -.
DR   PaxDb; Q5ZWE8; -.
DR   EnsemblBacteria; AAU27223; AAU27223; lpg1137.
DR   GeneID; 66490314; -.
DR   KEGG; lpn:lpg1137; -.
DR   PATRIC; fig|272624.6.peg.1195; -.
DR   eggNOG; ENOG5031DNH; Bacteria.
DR   HOGENOM; CLU_876589_0_0_6; -.
DR   OMA; AFMTFFK; -.
DR   Proteomes; UP000000609; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0044191; C:host cell mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR041000; Serine_protease.
DR   Pfam; PF18405; SLC25_like; 1.
PE   1: Evidence at protein level;
KW   Host membrane; Host mitochondrion; Hydrolase; Membrane; Protease;
KW   Reference proteome; Secreted; Serine protease; Virulence.
FT   CHAIN           1..322
FT                   /note="Serine protease Lpg1137"
FT                   /id="PRO_0000454157"
FT   ACT_SITE        68
FT                   /evidence="ECO:0000305|PubMed:28504273"
FT   MUTAGEN         68
FT                   /note="S->A: Abolished ability to catalyze degradation of
FT                   host STX17."
FT                   /evidence="ECO:0000269|PubMed:28504273"
FT   MUTAGEN         134
FT                   /note="S->A: Does not affect ability to catalyze
FT                   degradation of host STX17."
FT                   /evidence="ECO:0000269|PubMed:28504273"
SQ   SEQUENCE   322 AA;  35793 MW;  844933CCD8AA90D6 CRC64;
     MIQRGFTMQE RREKQGNNSP YLLTPYEMAN LVFKTGAISF TVSAGTQPFQ YLLNKLQFSQ
     SGTPSGLSGG LFRGMYRGFL PYAIAGQKRG AVAVTHKQTN KVTEEEEFEA PFRQRWWGTI
     FFSQADLLVS NGLSGKARLQ NVGVINAENF KWSLSNFWKL TSVNWGSRSF AGGVNFALIG
     FAGDYVSSFY KFDKDLYNKI LGGATSGVIA TLFTTAPNAY ADSKLLQTKV AENNRLITVS
     PYTMFGQMKS HVKAVGLKEA FMTFFKVSYL QQVAVRAPQA AITFALIFGM DEYMGPQPLK
     KVWPGRVEEL ESENPSPSPT KK