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Database: UniProt
Entry: A0A0S2DI04_LYSEN
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ID   A0A0S2DI04_LYSEN        Unreviewed;       516 AA.
AC   A0A0S2DI04;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   Name=nprV {ECO:0000313|EMBL:ALN58089.1};
GN   ORFNames=FE772_13715 {ECO:0000313|EMBL:QCW26563.1}, GLE_2741
GN   {ECO:0000313|EMBL:ALN58089.1};
OS   Lysobacter enzymogenes.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=69 {ECO:0000313|EMBL:ALN58089.1, ECO:0000313|Proteomes:UP000061569};
RN   [1] {ECO:0000313|EMBL:ALN58089.1, ECO:0000313|Proteomes:UP000061569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3 {ECO:0000313|EMBL:ALN58089.1,
RC   ECO:0000313|Proteomes:UP000061569};
RA   Kobayashi D.Y.;
RT   "Genome sequences of Lysobacter enzymogenes strain C3 and Lysobacter
RT   antibioticus ATCC 29479.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QCW26563.1, ECO:0000313|Proteomes:UP000308311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC36 {ECO:0000313|EMBL:QCW26563.1,
RC   ECO:0000313|Proteomes:UP000308311};
RA   Feng T.;
RT   "Intraspecies Signal LeDSF and Interspecies Signal Indole Synergistically
RT   Regulate the Twitching Motility of Lysobacter enzymogenes.";
RL   Submitted (MAY-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|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; CP013140; ALN58089.1; -; Genomic_DNA.
DR   EMBL; CP040656; QCW26563.1; -; Genomic_DNA.
DR   RefSeq; WP_057947780.1; NZ_CP040656.1.
DR   AlphaFoldDB; A0A0S2DI04; -.
DR   STRING; 69.GLE_2741; -.
DR   KEGG; lez:GLE_2741; -.
DR   PATRIC; fig|69.6.peg.2699; -.
DR   OrthoDB; 5378341at2; -.
DR   Proteomes; UP000061569; Chromosome.
DR   Proteomes; UP000308311; Chromosome.
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; 3.10.450.490; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR011096; FTP_domain.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000061569};
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..23
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           24..516
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5033768259"
FT   DOMAIN          69..117
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          226..365
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          368..513
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        358
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        441
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   516 AA;  55290 MW;  953BCD9FB7B80EF6 CRC64;
     MHRNVSALSL AVSFVLAAGA ADAAQVVDLH SVDAAKLDQQ YRAATAKSGT AAKAGVRHAE
     VIALDTESNL SELKSSVDAD GSRNYRYQQT YQGVPVFGEH VVVREDAQGK VRALFGRSVA
     GIAADLPKLD AKLSASQALG LAKAAAHGKR AAALQTRNEN SRKVVFVDDA GRARLAYAVD
     FVSDSVKGGE PSRPFAIVDA LDGKILKQWD GLNHAQVGTG PGGNQKIGQY EYGSGGRPFL
     DVTQNGSTYT FNTTNVKTVN LNNGTSGTTA YSYAGPRNTV RTINGAYSPL NDAHYFGKVV
     FDTYQAYVGL SPLTFQLTLR VHYSRNYENA FWDGRALTFG DGATTFHPLV SLDVVAHEAS
     HGYTEQQSGL IYSGQSGGIN ESYSDIAGEA AEFYSRGSND FLVGADIFKA AGRALRYFDD
     PTRDGRSIGH ARDYRNGLDV HYSSGVFNKA FYILARKPNW GTVKAFKAFA KANKDYWTPS
     TNFNQGGQGV RQAAADLGYS TADVIDAFNQ VGVTAQ
//
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