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Database: UniProt
Entry: A0A0W0VU76_9GAMM
LinkDB: A0A0W0VU76_9GAMM
Original site: A0A0W0VU76_9GAMM 
ID   A0A0W0VU76_9GAMM        Unreviewed;       558 AA.
AC   A0A0W0VU76;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Serine metalloprotease {ECO:0000313|EMBL:KTD23751.1};
GN   ORFNames=Llan_0532 {ECO:0000313|EMBL:KTD23751.1};
OS   Legionella lansingensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45067 {ECO:0000313|EMBL:KTD23751.1, ECO:0000313|Proteomes:UP000054869};
RN   [1] {ECO:0000313|EMBL:KTD23751.1, ECO:0000313|Proteomes:UP000054869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49751 {ECO:0000313|EMBL:KTD23751.1,
RC   ECO:0000313|Proteomes:UP000054869};
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   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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:KTD23751.1}.
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DR   EMBL; LNYI01000011; KTD23751.1; -; Genomic_DNA.
DR   RefSeq; WP_028372247.1; NZ_LT906451.1.
DR   AlphaFoldDB; A0A0W0VU76; -.
DR   STRING; 45067.Llan_0532; -.
DR   PATRIC; fig|45067.4.peg.558; -.
DR   eggNOG; COG1404; Bacteria.
DR   OrthoDB; 9790784at2; -.
DR   Proteomes; UP000054869; Unassembled WGS sequence.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Metalloprotease {ECO:0000313|EMBL:KTD23751.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000054869};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..558
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006915075"
FT   DOMAIN          162..429
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        169
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        210
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        394
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   558 AA;  59838 MW;  7E7FBDF57BA2EA57 CRC64;
     MHCKSGVVGL TFLILGQAAM ANDDTIRVIV KYKEPVSTLT ALQTQLSKST HLAIQALTPM
     AGGAYVVSFS IRGAQQSKNG VSTLDSVLQD LRKNEHVAYA VEDRVGRIQP LPTLKIEDLA
     DKLLSHDTQW DEFAAPGGIM LESAPYRHDG AWAHTTGKSA KPIVIAVLDT GVALNDSLVN
     NLVKDKQDNV WGWNFAANNR DISDETASYH GTHVAGTIAG YGDVMLGVGE DLKILPVKIP
     DGSGMFYESQ VINAIYWSVG GEVPGVPNNP YPAKVLNMSF GVDERPGKEI DHCDEALQEA
     LFYAREQGAV IAVAAGNDNR WEHYNAPAVC NGTIKVASTG PAGLRAYYSN YGPTVSFAAP
     GGDLRYGRKG GILSTVNPGG GYLNSGFDFY QGTSMASPHV AGVAGLIFAV RDGRISPESV
     EQILYATTHA FGKTADENKS CVGKKPCGHG ILDAENAIKA TMADYDLIIS APRITQLPKE
     PCRQKGAQSV ITVEQAGQEV RWITSKTFCG GDVIVKPVQL TTKTGQIIAD YGVMSYRLDD
     TRFKRCEIIG FDGIGCYL
//
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