LIE2_STREX
ID LIE2_STREX Reviewed; 1090 AA.
AC P83913;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Leupeptin-inactivating enzyme 2;
DE Short=LIE2;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=lieB;
OS Streptomyces exfoliatus (Streptomyces hydrogenans).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1905 {ECO:0000312|EMBL:AAQ73538.1};
RN [1] {ECO:0000312|EMBL:AAQ73538.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SMF13 {ECO:0000312|EMBL:AAQ73538.1};
RA Lee D.H., Lee K.J.;
RT "The role of metalloproteases (leupeptin-inactivating enzymes) in
RT morphological differentiation of Streptomyces exfoliatus SMF13.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A leucine-specific metalloprotease that plays a role in
CC controlling the amount of leupeptin during colony development. Degrades
CC leupeptin into three components, acetyl-leucine, leucine and argininal
CC (By similarity). {ECO:0000250|UniProtKB:P81715}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P81715};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P81715};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P81715}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P81715}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000305}.
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DR EMBL; AY335439; AAQ73538.1; -; Genomic_DNA.
DR AlphaFoldDB; P83913; -.
DR SMR; P83913; -.
DR MEROPS; M28.003; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR CDD; cd03876; M28_SGAP_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1090
FT /note="Leupeptin-inactivating enzyme 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000026853"
FT REGION 17..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 756
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 710
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P81715"
FT BINDING 722
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 722
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 757
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 785
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P81715"
FT BINDING 872
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT SITE 871
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT DISULFID 870..875
FT /evidence="ECO:0000250|UniProtKB:P80561"
SQ 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
