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Database: UniProt
Entry: Q6E9P5_LISMN
LinkDB: Q6E9P5_LISMN
Original site: Q6E9P5_LISMN 
ID   Q6E9P5_LISMN            Unreviewed;       510 AA.
AC   Q6E9P5;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 113.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   Name=mpl {ECO:0000313|EMBL:AAS85065.1};
GN   ORFNames=GHO09_14145 {ECO:0000313|EMBL:HAA8491649.1};
OS   Listeria monocytogenes.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1639 {ECO:0000313|EMBL:AAS85065.1};
RN   [1] {ECO:0000313|EMBL:AAS85065.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL 33031 {ECO:0000313|EMBL:AAS84855.1}, and NRRL 33106
RC   {ECO:0000313|EMBL:AAS85065.1};
RX   PubMed=15262937; DOI=10.1128/JB.186.15.4994-5002.2004;
RA   Ward T.J., Gorski L., Borucki M.K., Mandrell R.E., Hutchins J., Pupedis K.;
RT   "Intraspecific phylogeny and lineage group identification based on the prfA
RT   virulence gene cluster of Listeria monocytogenes.";
RL   J. Bacteriol. 186:4994-5002(2004).
RN   [2] {ECO:0000313|EMBL:ABG57035.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Lm19927 {ECO:0000313|EMBL:ABG57035.1};
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   [3] {ECO:0000313|EMBL:ABG57035.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Lm19927 {ECO:0000313|EMBL:ABG57035.1};
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.
RN   [4] {ECO:0000313|EMBL:ABY71503.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FSL S4-887 {ECO:0000313|EMBL:ABY71503.1};
RX   PubMed=18499533; DOI=10.1016/j.meegid.2008.04.006;
RA   Orsi R.H., Maron S.B., Nightingale K.K., Jerome M., Tabor H., Wiedmann M.;
RT   "Lineage specific recombination and positive selection in coding and
RT   intragenic regions contributed to evolution of the main Listeria
RT   monocytogenes virulence gene cluster.";
RL   Infect. Genet. Evol. 8:566-576(2008).
RN   [5] {ECO:0000313|EMBL:HAA8491649.1, ECO:0000313|Proteomes:UP000840567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sam_F526FDD3-C0F7-43DB-B204-E231FEF9C926
RC   {ECO:0000313|EMBL:HAA8491649.1};
RX   PubMed=30286803;
RA   Souvorov A., Agarwala R., Lipman D.J.;
RT   "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL   Genome Biol. 19:153-153(2018).
RN   [6] {ECO:0000313|EMBL:HAA8491649.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sam_F526FDD3-C0F7-43DB-B204-E231FEF9C926
RC   {ECO:0000313|EMBL:HAA8491649.1};
RG   NCBI Pathogen Detection Project;
RL   Submitted (OCT-2019) 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; AY512409; AAS84855.1; -; Genomic_DNA.
DR   EMBL; AY512444; AAS85065.1; -; Genomic_DNA.
DR   EMBL; DQ309886; ABG57035.1; -; Genomic_DNA.
DR   EMBL; EU372055; ABY71503.1; -; Genomic_DNA.
DR   EMBL; DAAEQL010000011; HAA8491649.1; -; Genomic_DNA.
DR   RefSeq; WP_012952055.1; NZ_WUEC01000009.1.
DR   MEROPS; M04.008; -.
DR   KEGG; lmom:IJ09_09350; -.
DR   PATRIC; fig|1639.1010.peg.2672; -.
DR   Proteomes; UP000840567; Unassembled WGS sequence.
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; 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, ECO:0000256|RuleBase:RU366073};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           25..510
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5015098247"
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          360..509
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        437
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   510 AA;  57411 MW;  FAC28FBB7AAEB270 CRC64;
     MKSKLICIIM VIAFQAHFTM TVKADSVGEE KLQNNTQAKK TPADLKALPD SCEAKDFYKN
     FKILDMTKDK LGVTHYTLAL SSGGYLTDND EIKVHVTPDN KITFINGDLQ QGQLRITNQI
     KITEKNAIEK AFEAIGQSEA HVKSYVGNPV KEKEIILNSR TKRLVYNIKL IFAEPEVASW
     IVQVDVETGA ILKKQNMLSE VERADTHKDF QALGKGANRL LQRPLHVMKI NDLFYLVDRT
     HKGLIRTFDL KHNTDTSFGK VVSNKTNMFT DPEFSSAVDA HFYASEVYEY YKNVHQLESL
     DGKGGEIDSF VHYGLNCNNA FWDGQEILYG DGDKKNFKPF SCAKTIVGHE LTHAVIQYSA
     GLEYEGQSGA LNESFADVFG YFIAPNHWLI GEDVCVRGSR DGRIRSIKDP DKYNQAAHMK
     DYESLPITEE GDWGGVHYNS GIPNKAAYNT ITKLGKEKTE QLYFRALKYY LTKKSQFTDA
     KKALQQAAKD LYGEDASKKV AEAWEAVGVN
//
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