ID   PRTA_LISMN              Reviewed;         510 AA.
AC   P34025;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 3.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Zinc metalloproteinase;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=mpl; Synonyms=prtA;
OS   Listeria monocytogenes.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1639;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LO28 / Serovar 1/2c;
RX   PubMed=1705239; DOI=10.1128/iai.59.3.1043-1049.1991;
RA   Mengaud J., Geoffroy C., Cossart P.;
RT   "Identification of a new operon involved in Listeria monocytogenes
RT   virulence: its first gene encodes a protein homologous to bacterial
RT   metalloproteases.";
RL   Infect. Immun. 59:1043-1049(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-272.
RC   STRAIN=12067;
RX   PubMed=1937753; DOI=10.1128/iai.59.11.3945-3951.1991;
RA   Rasmussen O.F., Beck T., Olsen J.E., Dons L., Rossen L.;
RT   "Listeria monocytogenes isolates can be classified into two major types
RT   according to the sequence of the listeriolysin gene.";
RL   Infect. Immun. 59:3945-3951(1991).
CC   -!- FUNCTION: Probably linked to the pathogenesis of listerial infection.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: The mpl and the listeriolysin genes being physically linked,
CC       their expression may be regulated in a similar manner.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR   EMBL; X60035; CAA42640.1; -; Genomic_DNA.
DR   PIR; B60280; B60280.
DR   RefSeq; WP_010958689.1; NZ_WUDT01000002.1.
DR   AlphaFoldDB; P34025; -.
DR   SMR; P34025; -.
DR   STRING; 1027396.LMOSA_10960; -.
DR   MEROPS; M04.008; -.
DR   eggNOG; COG3227; Bacteria.
DR   OrthoDB; 1465483at2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR025711; PepSY.
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; PF03413; PepSY; 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   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal;
KW   Virulence; Zinc; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..200
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000028634"
FT   CHAIN           201..510
FT                   /note="Zinc metalloproteinase"
FT                   /id="PRO_0000028635"
FT   ACT_SITE        350
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        437
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         373
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CONFLICT        47
FT                   /note="T -> A (in Ref. 2; CAA42640)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="T -> A (in Ref. 2; CAA42640)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   510 AA;  57569 MW;  C166CB56515BB175 CRC64;
     MKSKLICIIM VIAFQAHFNM AVKADSVGEE RLRNNIQAKR NPADLKTLPD SCEAKDFYKN
     FKILDMTKDK LGVTHYTLAL SSDGYLTDND EIKVHVTPDN KITFINGDLQ QGQLRITNQI
     KITEKNAIEK AFEAIGQSEA HVKSYIGNPV KEKEIIINSR TKRLVYNIKL IFAEPEVASW
     IIQVDAETGA ILKKQNMLSE VERADTHKDF QALGKGANRL LQRPLHVMKI NDLFYLVDRT
     HKGLIRTFDL NHKTDASFGK VVSNKTNMFT DPEFSSAVDA HFYASEVYDY YKNVHQLESL
     DGKGGEIDSF VHYGLNCNNA FWDGREILYG DGDKKNFKPF SCAKTIVGHE LTHAVIQYSA
     GLEYEGQSGA LNESFADVFG YFIAPNHWLI GEDVCVRGLR DGRIRSIKDP DKYNQAAHMK
     DYESLPITEE GDWGGVHFNS GIPNKAAYNT ITKLGKEKTE QLYFRALKYY LTKKAQFTDA
     KKALQQAAKD LYGEDASKKV AEAWEAVGVN