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
//