UniProt: A0A0S2DE27

Database: UniProt
Entry: A0A0S2DE27_LYSEN

LinkDB:  A0A0S2DE27_LYSEN 
Original site:  A0A0S2DE27_LYSEN

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Ontology (4)   
   GO (4)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (3)   
All databases (15)   

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ID   A0A0S2DE27_LYSEN        Unreviewed;       596 AA.
AC   A0A0S2DE27;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=GLE_1464 {ECO:0000313|EMBL:ALN56821.1};
OS   Lysobacter enzymogenes.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=69 {ECO:0000313|EMBL:ALN56821.1, ECO:0000313|Proteomes:UP000061569};
RN   [1] {ECO:0000313|EMBL:ALN56821.1, ECO:0000313|Proteomes:UP000061569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3 {ECO:0000313|EMBL:ALN56821.1,
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.
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; ALN56821.1; -; Genomic_DNA.
DR   RefSeq; WP_057946796.1; NZ_CP013140.1.
DR   AlphaFoldDB; A0A0S2DE27; -.
DR   STRING; 69.GLE_1464; -.
DR   KEGG; lez:GLE_1464; -.
DR   PATRIC; fig|69.6.peg.1445; -.
DR   OrthoDB; 5378341at2; -.
DR   Proteomes; UP000061569; 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; 3.10.450.490; -; 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..20
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           21..596
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023094623"
FT   DOMAIN          116..162
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          259..403
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          415..595
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        397
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        497
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   596 AA;  61967 MW;  2A23224467EC75C8 CRC64;
     MQPKIALLGG AILAAIAVLA SQSSSIGATA GATADARDAA RPNAGARAAV ADAHAANARH
     SSPFAQLAAA TGARAGSELA SASSSEAQAD ASPAAARARG LLEGAAGDQL HRVAADGFRA
     RDVMIDRDGT EHVRMERSYQ GLPVVGGDFV VHSRDGQLLS ISQGDDMRTL ARPALKPAIG
     ADRARVEAGA AFDGTASSVS QPQLVVFARG VAPTLAYQVD VRGERNNDPA PGNLSYFIDA
     GNGTLLHEED HVHAAAANGT GKTLTLGNVG IVTNSVGGGF EMTDPSRGNG QTLDAGNGNS
     ASGTLFKDAD NVWGNNATSD RATAAADAHY GVAATWDYYK NVHGRNGIKN DGRGVKSYIH
     YKTNLVNAYW DGSSMLYGDG DGTTYRPLVA LDVAGHEMTH GVTGATARLG YYNIKDSGGI
     NEGISDIFGT LVEFSVANAN DPGDYLIGEE VYISNPGDKK ALRLMFKQDA DGASKVCYPS
     GGFTASQTYA RGPFDPHYTS GVLNRVFYLG SEGANVPAGF NYTKAQMVCN GDTAIAGIGR
     NKMGAIMYRA LTRYFVSSTT YPQARTWTLQ AATDLYGANS AEYAALARVW SAVNVN
//

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