ID   MSPA_LEGLO              Reviewed;         529 AA.
AC   P55110;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Zinc metalloproteinase MspA;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=mspA;
OS   Legionella longbeachae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33462 / DSM 10572 / NCTC 11477 / Long Beach 4 / Serogroup 1;
RA   Lim I.S.L., Olesnicky N., Heuzenroeder M.W.;
RT   "Identification, characterization and distribution of an analogue of the
RT   Legionella pneumophila major secretory protein in L. longbeachae.";
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR   EMBL; X83035; CAA58144.1; -; Genomic_DNA.
DR   PIR; S52759; S52759.
DR   RefSeq; WP_003635269.1; NZ_CP045308.1.
DR   AlphaFoldDB; P55110; -.
DR   SMR; P55110; -.
DR   MEROPS; M04.006; -.
DR   OMA; TVHTRYD; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.390.10; -; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR023612; Peptidase_M4.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR001570; Peptidase_M4_C_domain.
DR   InterPro; IPR013856; Peptidase_M4_domain.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Signal; Zinc; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..204
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028636"
FT   CHAIN           205..529
FT                   /note="Zinc metalloproteinase MspA"
FT                   /id="PRO_0000028637"
FT   ACT_SITE        366
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        451
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         365
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         389
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   529 AA;  58713 MW;  D2D2B721AE90A848 CRC64;
     MHHNYYLSPL AVALALGMVS PAKAADPILL QNASFSEVKQ KFALSTQGVA VAKDSLSFVS
     EHTDRNKVTH VRMQQKYVGF PVYGGYAIMH SMNTAKSLAA TTQSTVEMNG VVYQGLQTEL
     GQPDASFVQN ADKALQQFKA KYANQNVGDE KVIPMVYIDK DNQAHWAYKV SIRVNHLDKA
     PERPTAIIDA RTQQPFVQWN DIKTERVSVK GSGFGGNKKM GYYEFGKDFP YLDLTRDANN
     ATCYMENESV KVIDMKHKYS SVKAAMSFAC STTDSDIYST GYREDNGALS PSNDALYAGY
     VIKHMYTDWY GVNVLSNSNG SPMQLVMRVH YGDGYENAYW DGEQMTFGCG DRMMYPLVSL
     GVGAHEISHG FTEQHSGLEY YGQSGGMNES FSDMAAQAAE HYSVGKSSWQ IGGEIMKESS
     GYDALRYMDK PSRDGESIDT ADEYYSGLDV HYSSGVYNHL FYILATKPNW DTRKAFDVMV
     KANMDYWTPY SSFDEGGCGV LSAAKDLGFS LNDVKSSLQA VAINYSKCH