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Database: UniProt
Entry: B9UXU7_LISMN
LinkDB: B9UXU7_LISMN
Original site: B9UXU7_LISMN 
ID   B9UXU7_LISMN            Unreviewed;       510 AA.
AC   B9UXU7;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   Name=mpl {ECO:0000313|EMBL:ACM43591.1};
GN   ORFNames=lmo0203 {ECO:0000313|EMBL:ACM43591.1};
OS   Listeria monocytogenes.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1639 {ECO:0000313|EMBL:ACM43591.1};
RN   [1] {ECO:0000313|EMBL:ACM43591.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL_B-33371 {ECO:0000313|EMBL:ACM43591.1};
RX   PubMed=18931295; DOI=10.1128/AEM.01127-08;
RA   Ward T.J., Ducey T.F., Usgaard T., Dunn K.A., Bielawski J.P.;
RT   "Multilocus genotyping assays for single nucleotide polymorphism-based
RT   subtyping of Listeria monocytogenes isolates.";
RL   Appl. Environ. Microbiol. 74:7629-7642(2008).
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; FJ041128; ACM43591.1; -; Genomic_DNA.
DR   RefSeq; WP_070241423.1; NZ_MKNN01000006.1.
DR   AlphaFoldDB; B9UXU7; -.
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, 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_5023154425"
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;  57345 MW;  70D8E418D7012E46 CRC64;
     MKSKLICIIM VIAFQAHFTM AVKADSVGEE RLQNNIQAKR NPADLKALPD SCEAKDFYKN
     FKILDMTKDK LGVTHYTLAL SSGGYLTDND EIKVHVTPDN KITFINGDLQ QGQLKITNQI
     KMTEKNAIEK AFEAIGQSEA HVKSYIGNPV KEKEIIINSR TKRLVYNIKL IFAEPEVASW
     IIQVDAETGA ILKKQNMLSE VERADTHKDF QALGKGANRL LQRPLHVMKI NDLFYLVDRT
     HKGLIRTFDL NHKTDASFGK VVSNKTNMFT DPEFSSAVDA HFYASEVYEY YKNVHQLESL
     DGKGGEIDSF VHYGLNCNNA FWDGREILYG DGDKKNFKPF SCAKTIVGHE LTHAVIQYSA
     GLEYEGQSGA LNESFADVFG YFIAPNHWLI GEDVCVRGSR DGRIRSIKDP DKYNQAAHMK
     DYASLPITEE GDWGGVHFNS GIPNKAAYNT ITKLGKEKTE QLYFRALKYY LTKKAQFTDA
     KKALQQAAKD LYGEDASIKV AEAWEAVGVN
//
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