ID   D3HIY5_LEGLN            Unreviewed;       605 AA.
AC   D3HIY5;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Putative zinc-dependent metallopeptidase {ECO:0000313|EMBL:CBJ12366.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:CBJ12366.1};
GN   OrderedLocusNames=LLO_1982 {ECO:0000313|EMBL:CBJ12366.1};
OS   Legionella longbeachae serogroup 1 (strain NSW150).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ12366.1, ECO:0000313|Proteomes:UP000001060};
RN   [1] {ECO:0000313|EMBL:CBJ12366.1, ECO:0000313|Proteomes:UP000001060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSW150 {ECO:0000313|EMBL:CBJ12366.1,
RC   ECO:0000313|Proteomes:UP000001060};
RX   PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA   Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA   Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA   Etienne J., Hartland E., Buchrieser C.;
RT   "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT   unique strategies to cause Legionnaires' disease.";
RL   PLoS Genet. 6:E1000851-E1000851(2010).
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DR   EMBL; FN650140; CBJ12366.1; -; Genomic_DNA.
DR   RefSeq; WP_003636799.1; NC_013861.1.
DR   AlphaFoldDB; D3HIY5; -.
DR   STRING; 661367.LLO_1982; -.
DR   KEGG; llo:LLO_1982; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_6; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000001060; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06461; M2_ACE; 1.
DR   Gene3D; 1.10.1370.30; -; 1.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:CBJ12366.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:CBJ12366.1};
KW   Protease {ECO:0000313|EMBL:CBJ12366.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001060};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..605
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003045826"
SQ   SEQUENCE   605 AA;  70232 MW;  E019D6FAA1E44253 CRC64;
     MKHYYKIILI SSYLLLSCQN SGSNLNTNAA EAQKFIDNYT KQYVQFYTSA KNARWQSNIE
     IKPNDFTNTK IAQKADKALA VFVGSKENIK GAQKYLNPKY KLTKIQVKQL ELILYSAANS
     PQEVAELVEK RIQAEVEQIY KLYGYQYKLD GKKIGVNHID CILKKESNLN KRLSAWEASK
     QVGPTLKAGL INLRNLRNQT VQALGYPDFF TYQVNSYHMS TDEMMQTLEG LMRELYPLYR
     ELHTWMRYEL AKRYGVNTVP KYLPAHWLPN RWGQDWSSML KDKSINIDDI LKNKSPDWIM
     KSAESLYVSL GYPKLPATFW KKSNLYPYPS NSSIKKNNHA SAWHIDLNQD IRIIMSLESN
     AKSFRTAHHE LGHIYYYLTY TNKDVPPLLR KGANRAFHEA IGTMMGLAAR KKPYLVERGL
     IDNSVEIDNM YTLLKEALNS VVFIFFSAGT MSHFEKAMYV DNLSPDQFNV KWWELAKKYQ
     GIEPPFIRGE EYCDAATKTH INNDPAQYYD YALSYVLLYQ LHNHIAKNIL HQDPHATNYF
     GQQAIGDFLL HIMRHGASKD WREVLKESTG DELSAKAMLE YFQPLVEWLH EQNKGRNYSL
     PEIMV
//