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Leupeptin-inactivating enzyme 2 (LIE2) (EC 3.4.24.-)

 LIE2_STREX              Reviewed;        1090 AA.
P83913;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
24-MAY-2004, sequence version 1.
10-MAY-2017, entry version 63.
RecName: Full=Leupeptin-inactivating enzyme 2;
Short=LIE2;
EC=3.4.24.-;
Flags: Precursor;
Name=lieB;
Streptomyces exfoliatus (Streptomyces hydrogenans).
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1905 {ECO:0000312|EMBL:AAQ73538.1};
[1] {ECO:0000312|EMBL:AAQ73538.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SMF13 {ECO:0000312|EMBL:AAQ73538.1};
Lee D.H., Lee K.J.;
"The role of metalloproteases (leupeptin-inactivating enzymes) in
morphological differentiation of Streptomyces exfoliatus SMF13.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: A leucine-specific metalloprotease that plays a role in
controlling the amount of leupeptin during colony development.
Degrades leupeptin into three components, acetyl-leucine, leucine
and argininal (By similarity). {ECO:0000250|UniProtKB:P81715}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P81715};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000250|UniProtKB:P81715};
-!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P81715}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P81715}.
-!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
{ECO:0000305}.
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EMBL; AY335439; AAQ73538.1; -; Genomic_DNA.
ProteinModelPortal; P83913; -.
SMR; P83913; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008237; F:metallopeptidase activity; ISS:UniProtKB.
GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
CDD; cd09597; M4_neutral_protease; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR007484; Peptidase_M28.
InterPro; IPR023612; Peptidase_M4.
InterPro; IPR001570; Peptidase_M4_C_domain.
InterPro; IPR013856; Peptidase_M4_domain.
Pfam; PF04389; Peptidase_M28; 1.
Pfam; PF01447; Peptidase_M4; 1.
Pfam; PF02868; Peptidase_M4_C; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
3: Inferred from homology;
Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
Secreted; Signal; Zinc.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 1090 Leupeptin-inactivating enzyme 2.
{ECO:0000305}.
/FTId=PRO_0000026853.
ACT_SITE 756 756 Proton acceptor.
{ECO:0000250|UniProtKB:P80561}.
METAL 710 710 Zinc 1; catalytic.
{ECO:0000250|UniProtKB:P81715}.
METAL 722 722 Zinc 1; catalytic.
{ECO:0000250|UniProtKB:P80561}.
METAL 722 722 Zinc 2; catalytic.
{ECO:0000250|UniProtKB:P80561}.
METAL 757 757 Zinc 2; catalytic.
{ECO:0000250|UniProtKB:P80561}.
METAL 785 785 Zinc 1; catalytic.
{ECO:0000250|UniProtKB:P81715}.
METAL 872 872 Zinc 2; catalytic.
{ECO:0000250|UniProtKB:P80561}.
SITE 871 871 Transition state stabilizer.
{ECO:0000250|UniProtKB:P80561}.
DISULFID 870 875 {ECO:0000250|UniProtKB:P80561}.
SEQUENCE 1090 AA; 111736 MW; DA9B2A32D9E700A1 CRC64;
MAAMALTASL AGALAGTASA AQQAQPSPSQ KDTPAARAVA AADQAVDSGL DSLVNSSQEQ
YERRLVTPWV KDLYSVSYER SYRGLPVVGG DAVVLADGTG KVRALQSASS VRIDVSTQAS
VSAKDAESTS RAKLVSVDKV ESSRLVVRLK DDKPVLAWET VLSGRTKTAP SKLHVFVDAR
TGAFVDSYDE VVAGTGNSKW NGPGPVTIDT TNSGSTYTLR DPVRTGLSCA DYSTGTVFSK
SSDSWGTGNP TSKETGCVDL MFAAQKQWDM LSQWLGRNGV SGNGRSFPAK VGLSDLNAYW
DGSSVTIGRN SAGEWIAGID VVAHEYGHAI DSNTPGGTSG QESGLGEATG DIFGALTEAF
ANEPAPYDTP DYTVGEVINL QGRGPIRNMY NPPAVNNDPA CYSSAIPGTE VHAAAGPLNH
WFYLLAEGTS PGGGKPNSST CNGTSLTGVG VQNAGKIFYG GMLLKTSSMS YKKYRTATLS
SAKSLDATCD LFNKTKAAWD GISVPAQTAD PTCTPSGQNN DFSMSLSPSS GTVQQGASVT
TTVGTTVTTG NAQSVTLTAS GLPAGVSASF NPATVQSGQS SVLTLTATAN AAPGASTIVV
KGQGASLSHT VDYALNVGGT QPGNDPPDID VANVQAHLTQ FNTIASQNGG HRRAGSAGYT
QSLAYVKGKL QAAGYTVTEQ NCTSCTYPSN NLIADWPGGP ADQTVMFGAH LDGVSAGPGI
NDNGSGSATL LENALVLAQK NPTMTKHVRF AWWTDEEQGL NGSEFYVNQL SSAQRSAIKG
YYNFDMVGST NGGYFINNVN STTAAPLKAY WTSLNLAPEE NTEGQGRSDD YSFQQAGIPT
SGYAAGASAR KTSAQATKWG GTANAAYDPC YHSSCDTTNN INATVLNRSA DGVAYAVWKQ
AVGGETPAQD FSVAVSPSAG SAAPGGSTSA TVNTATVSGA AQTVALSVSG APAGVTATLS
PTSVQSGSSS ALSVQVGAST APGTYTLTVT GSGTVSHTST YSLTVTGGGS CTPRQLVTNG
GFESGSSPWS ATAGQTLETL SNLNANSGYA EKSYDLSQFA GQTVTLKFTG TEDQSLQTSF
VVDDVTVQVS


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