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Alpha-lytic protease L1 (EC 3.4.21.12) (Alpha-lytic endopeptidase L1) (Fragments)

 PRLA_LYSSX              Reviewed;          62 AA.
P85142;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
15-MAY-2007, sequence version 1.
08-MAY-2019, entry version 33.
RecName: Full=Alpha-lytic protease L1;
EC=3.4.21.12;
AltName: Full=Alpha-lytic endopeptidase L1;
Flags: Fragments;
Lysobacter sp. (strain XL1).
Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
Xanthomonadaceae; Lysobacter.
NCBI_TaxID=186334;
[1] {ECO:0000305}
PROTEIN SEQUENCE.
PubMed=15193123; DOI=10.1023/B:BIRY.0000029847.40511.26;
Muranova T.A., Krasovskaya L.A., Tsfasman I.M., Stepnaya O.A.,
Kulaev I.S.;
"Structural investigations and identification of the extracellular
bacteriolytic endopeptidase L1 from Lysobacter sp. XL1.";
Biochemistry (Mosc.) 69:501-505(2004).
[2] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
Muranova T.A., Stepnaya O.A., Tsfasman I.M., Kulaev I.S.;
"Identification of extracellular bacteriolytic enzymes from Lysobacter
sp. XL1.";
Submitted (APR-2007) to UniProtKB.
-!- FUNCTION: Has bacteriolytic activity. {ECO:0000269|Ref.2}.
-!- CATALYTIC ACTIVITY:
Reaction=Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial
cell walls, elastin and other proteins.; EC=3.4.21.12;
Evidence={ECO:0000250|UniProtKB:P00778, ECO:0000269|Ref.2};
-!- ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride
(PMSF) and p-chloromercuribenzoate (PCMB). {ECO:0000269|Ref.2}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8.0. Active from pH 7.0 to 11.0.
{ECO:0000269|Ref.2};
Temperature dependence:
Optimum temperature is 70 degrees Celsius. {ECO:0000269|Ref.2};
-!- SUBUNIT: Monomer. {ECO:0000269|Ref.2}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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SMR; P85142; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
InterPro; IPR009003; Peptidase_S1_PA.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
Hydrolase; Protease; Secreted; Serine protease.
CHAIN 1 >62 Alpha-lytic protease L1.
/FTId=PRO_0000287680.
ACT_SITE 48 48 Charge relay system.
DISULFID 17 ? {ECO:0000250|UniProtKB:P00778,
ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 42 ? {ECO:0000250|UniProtKB:P00778,
ECO:0000255|PROSITE-ProRule:PRU00274}.
NON_CONS 23 24 {ECO:0000303|PubMed:15193123}.
NON_CONS 26 27 {ECO:0000303|PubMed:15193123}.
NON_CONS 54 55 {ECO:0000303|PubMed:15193123}.
NON_CONS 58 59 {ECO:0000303|PubMed:15193123}.
NON_TER 62 62 {ECO:0000303|PubMed:15193123}.
SEQUENCE 62 AA; 6611 MW; 2C602878C9E3BFDE CRC64;
VNVLGGIEYS INNATLCSVG FSVRVFNYAE GAVRGLTQGN ACMGRGDSGG SWFTLFERQY
GL


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[UCHL1] Ubiquitin carboxyl-terminal hydrolase isozyme L1 (UCH-L1) (EC 3.4.19.12) (Neuron cytoplasmic protein 9.5) (PGP 9.5) (PGP9.5) (Ubiquitin thioesterase L1)
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[tat] Protein Tat (Transactivating regulatory protein)
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Bibliography :
[15193123] Structural investigations and identification of the extracellular bacteriolytic endopeptidase L1 from Lysobacter sp. XL1.