ID   A0A0W0WMD5_9GAMM        Unreviewed;       738 AA.
AC   A0A0W0WMD5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Ser-Thr-rich glycosyl-phosphatidyl-inositol-anchored membrane family protein {ECO:0000313|EMBL:KTD33270.1};
GN   ORFNames=Lnau_2918 {ECO:0000313|EMBL:KTD33270.1};
OS   Legionella nautarum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD33270.1, ECO:0000313|Proteomes:UP000054725};
RN   [1] {ECO:0000313|EMBL:KTD33270.1, ECO:0000313|Proteomes:UP000054725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD33270.1,
RC   ECO:0000313|Proteomes:UP000054725};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KTD33270.1}.
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DR   EMBL; LNYO01000024; KTD33270.1; -; Genomic_DNA.
DR   RefSeq; WP_058505875.1; NZ_LNYO01000024.1.
DR   AlphaFoldDB; A0A0W0WMD5; -.
DR   STRING; 45070.Lnau_2918; -.
DR   PATRIC; fig|45070.6.peg.3079; -.
DR   OrthoDB; 5242130at2; -.
DR   Proteomes; UP000054725; Unassembled WGS sequence.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   Pfam; PF13583; Reprolysin_4; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00023049}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..738
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006915653"
FT   DOMAIN          306..416
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
SQ   SEQUENCE   738 AA;  79109 MW;  D4F530E3840F8024 CRC64;
     MTRMFIAVFL LAFSSLVSAQ NYKVINNIIK DVKPASIPLD GKRLIQAKHY RTVEININRL
     YSALEKVPLR GGLRAGVPVL IELPLPDGSM RKYRVVENTT MHPQLAAKFP EIKTYDGYGV
     GKSAELVKFD ITPHGFHAMI LSPGKNTVFI DPLEKDNTQY YMVYKQKDFV SKKNMKCGVT
     GQSKPIKHLR QLRPSANFNA CNLKTYRLAM AATAQYTAFH GGTVPLALAA EVTTVNRVNA
     VYETDMAITL QIIPNNDQII YTDPLTQPYT SGRPPILLVE NQANVTAVIG AANYDIGHVV
     DAAGSGLATL GCVCNSSEKA EGVTGGEQPI GDPFDVDFLA HEIGHQFGAN HTQDNDCKRN
     PATAVEPGSG STIMGYAGIC PPNVQMNSSP YFHGISLQEM GDFVSGQGGT CPVETPIPQA
     PTILSTNGFA VVPANTPFAL TTIATNNGGN NVLTYTWEQM DNQISIQPPL SDSPDGPNFR
     SISPSVSPTR FFPNLAAIAN NGPFTWEVVP SVTRTMNFRT TVRANTPGGS CNSYVDVTLT
     TDASSGPFIL TYPTAPNIVW LSGAQLPVTW NVANTDVPPV NATVVDILLS IDGGLSYPFA
     LLSAVPNNGT AMVTVPAINT ASARIMVRSA NGTFFTTSAN NFSIGLSSPT APVLLRADRN
     RLNPTVAFIY YAGLDSAVFN NDVYLVNGVP GAIAALDRAH GRFVISNLFL PQQQVVSITV
     VRGGFSQTSN AITIPSIL
//