ID Q6E8Z3_LISMN Unreviewed; 510 AA.
AC Q6E8Z3;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN Name=mpl {ECO:0000313|EMBL:AAS85317.1};
GN ORFNames=lmo0203 {ECO:0000313|EMBL:ACM43521.1};
OS Listeria monocytogenes.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1639 {ECO:0000313|EMBL:AAS85317.1};
RN [1] {ECO:0000313|EMBL:AAS85317.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 33191 {ECO:0000313|EMBL:AAS85317.1};
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:ACM43521.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL_B-33330 {ECO:0000313|EMBL:ACM43521.1}, and NRRL_B-33378
RC {ECO:0000313|EMBL:ACM43640.1};
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).
RN [3] {ECO:0000313|EMBL:AAS85317.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 33191 {ECO:0000313|EMBL:AAS85317.1};
RA Ward T.J., Gorski L., Borucki M.K., Mandrell R.E., Hutchins J., Pupedis K.;
RL Submitted (AUG-2008) 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; AY512486; AAS85317.1; -; Genomic_DNA.
DR EMBL; FJ041118; ACM43521.1; -; Genomic_DNA.
DR EMBL; FJ041135; ACM43640.1; -; Genomic_DNA.
DR RefSeq; WP_070212175.1; NZ_VTKP01000003.1.
DR AlphaFoldDB; Q6E8Z3; -.
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_5009344844"
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; 57400 MW; 8EBB20CA29730274 CRC64;
MKSKLICIIM VIAFQAHFTM TVKADSVGEE RLQNNIQAKR NPADLKALPD SCEAKDFYKN
FKILDMTKDK LGVTHYTLAL SSGGYLTDND EIKVHVTPDN KITFINGDLQ QGQLRITNQI
KITEKNAIEK 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 LYGEDASKKV AEAWEAVGVN
//
