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Database: UniProt
Entry: Q0ZPA4_LISMN
LinkDB: Q0ZPA4_LISMN
Original site: Q0ZPA4_LISMN 
ID   Q0ZPA4_LISMN            Unreviewed;       511 AA.
AC   Q0ZPA4;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   Name=mpl {ECO:0000313|EMBL:ABG57040.1};
OS   Listeria monocytogenes.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1639 {ECO:0000313|EMBL:ABG57040.1};
RN   [1] {ECO:0000313|EMBL:ABG57040.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Lm26686 {ECO:0000313|EMBL:ABG57040.1};
RA   Papageorgiou N., Tselentis Y., Scoulica E.;
RT   "Nucleotide sequence diversity of prfA gene cluster of Listeria
RT   monocytogenes strains of clinical and food origin.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABG57040.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Lm26686 {ECO:0000313|EMBL:ABG57040.1};
RA   Papageorgiou N., Tselentis Y., Scoulica E.;
RT   "Nucleotide sequence of actA genes from clinical and environmental Listeria
RT   monocytogenes isolates.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular zinc metalloprotease.
CC       {ECO:0000256|RuleBase:RU366073}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU366073};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU366073}.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family.
CC       {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
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DR   EMBL; DQ309974; ABG57040.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0ZPA4; -.
DR   MEROPS; M04.008; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09597; M4_TLP; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 3.10.450.40; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 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   PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR   PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
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   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU366073};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW   Secreted {ECO:0000256|RuleBase:RU366073};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          60..109
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          121..194
FT                   /note="PepSY"
FT                   /evidence="ECO:0000259|Pfam:PF03413"
FT   DOMAIN          214..357
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          362..510
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        350
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        438
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   511 AA;  57610 MW;  BACB51264F194033 CRC64;
     MKSKLICIIM VIAFQAHFNM AVKADSVGEE RLRNNIQAKR NPADLKALPD SCEAKDFYKN
     FKILDMTKDK LGVTHYTLAL SSEGYLTDND 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
     GGLEYEGQSG ALNESFADVF GYFIAPNHWL IGEDVCVRGL RDGRIRSIKD PDKYNQAAHM
     KDYESLPITE EGDWGGVHFN SGIPNKAAYN TITKLGKEKT EQLYFRALKY YLTKKAQFTD
     AKKALQQAAK DLYGEDASKK VAEAWEAVGV N
//
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