LIE1_STREX
ID LIE1_STREX Reviewed; 438 AA.
AC P81715;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Leupeptin-inactivating enzyme 1;
DE Short=LIE1;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=lieA;
OS Streptomyces exfoliatus (Streptomyces hydrogenans).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1905 {ECO:0000305};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SMF13;
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.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 38-51.
RC STRAIN=SMF13;
RX PubMed=9531495; DOI=10.1042/bj3310539;
RA Kim I.S., Kim Y.B., Lee K.J.;
RT "Characterization of the leupeptin-inactivating enzyme from Streptomyces
RT exfoliatus SMF13 which produces leupeptin.";
RL Biochem. J. 331:539-545(1998).
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 Has a strict preference for leucine at the P1 site.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P80561};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P80561};
CC -!- ACTIVITY REGULATION: Activity is inhibited by metalloprotease
CC inhibitors and activated by Mg(2+) and Ca(2+).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0.;
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000305}.
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DR EMBL; AY335438; AAQ73537.1; -; Genomic_DNA.
DR AlphaFoldDB; P81715; -.
DR SMR; P81715; -.
DR MEROPS; M28.003; -.
DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd03876; M28_SGAP_like; 1.
DR InterPro; IPR029514; Ape3.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR PANTHER; PTHR12147:SF17; PTHR12147:SF17; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Secreted; Signal; Zinc.
FT SIGNAL 1..37
FT /evidence="ECO:0000269|PubMed:9531495"
FT CHAIN 38..438
FT /note="Leupeptin-inactivating enzyme 1"
FT /id="PRO_0000026852"
FT DOMAIN 321..438
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 125
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 137
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 137
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 172
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 200
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 287
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 286
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT DISULFID 285..290
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CONFLICT 50
FT /note="K -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 45302 MW; 8C48D39914DD977E CRC64;
MSLSVSRRLA AVTAFAVAGL FASAVPAALA APSAVAAAPT PPDIPLANVK AHLSQLSTIA
ANNGGNRAHG RAGYKASIDY VKGKLDAAGF TTTLQTFTSS GATGYNLIAD WPGGDPNSVL
MAGSHLDSVT SGAGINDNGS GSAAVLETAL AVSRAGLQPT KHLRFGWWGA EELGLIGSKY
YVNNLPAAEK AKISGYLNFD MIGSPNPGYF VYDDDPTIEQ TFKNYYAGLG VPTEIETEGD
GRSDHAPFKN AGIPVGGLFS GADYTKTAAQ AQKWGGTSGQ AFDRCYHSSC DSLTNINDTA
LDRNSDAVAY AIWTLGAGTP VPPGQSFENT ADVNVPDSPA AAVSSPITVS GVTGNAPATT
KVDVNIVHTY RGDLVVDLVA PDGTVYNLHN RSGGSADNLV QTYTVNASSE VANGVWNLRV
KDTAAQDVGY INSWKITF
