ID   LYSC_LYSEN              Reviewed;         269 AA.
AC   Q7M135;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Lysyl endopeptidase;
DE            EC=3.4.21.50;
DE   AltName: Full=Lys-C;
OS   Lysobacter enzymogenes.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=69;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Mentele R., Eckerskorn C., Kellermann J., Strupat K., Hagmann J.,
RA   Lottspeich F.;
RL   Submitted (JUN-1997) to the PIR data bank.
CC   -!- FUNCTION: Highly specific endopeptidase that hydrolyzes lysyl bonds
CC       including the Lys-Pro bond.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro.;
CC         EC=3.4.21.50;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- BIOTECHNOLOGY: Sold under the name 'Endoproteinase Lys-C' by Roche.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; S77957; S77957.
DR   PDB; 4NSV; X-ray; 0.90 A; A/B=1-266.
DR   PDB; 4NSY; X-ray; 1.10 A; A/B=1-266.
DR   PDBsum; 4NSV; -.
DR   PDBsum; 4NSY; -.
DR   AlphaFoldDB; Q7M135; -.
DR   SMR; Q7M135; -.
DR   MEROPS; S01.280; -.
DR   PRIDE; Q7M135; -.
DR   BRENDA; 3.4.21.50; 3118.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   SUPFAM; SSF50494; SSF50494; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Protease; Secreted; Serine protease.
FT   CHAIN           1..269
FT                   /note="Lysyl endopeptidase"
FT                   /id="PRO_0000093854"
FT   ACT_SITE        57
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        113
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        194
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        6..216
FT                   /evidence="ECO:0000250"
FT   DISULFID        12..80
FT                   /evidence="ECO:0000250"
FT   DISULFID        36..58
FT                   /evidence="ECO:0000250"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   HELIX           21..24
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          25..30
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          33..41
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          51..55
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   HELIX           63..67
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   TURN            86..89
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          98..101
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          103..109
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   TURN            110..113
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          114..121
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          130..135
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          144..148
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          156..160
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          165..168
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          173..181
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          197..199
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          203..211
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          223..229
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   HELIX           230..235
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   HELIX           240..242
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   HELIX           245..248
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   TURN            249..251
FT                   /evidence="ECO:0007829|PDB:4NSV"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:4NSV"
SQ   SEQUENCE   269 AA;  27961 MW;  2072A25C142A30A6 CRC64;
     GVSGSCNIDV VCPEGNGHRD VIRSVAAYSK QGTMWCTGSL VNNSANDKKM YFLTANHCGM
     TTAAIASSMV VYWNYQNSTC RAPGSSSSGA NGDGSLAQSQ TGAVVRATNA ASDFTLLELN
     TAANPAYNLF WAGWDRRDQN FAGATAIHHP NVAEKRISHS TVATEISGYN GATGTSHLHV
     FWQASGGVTE PGSSGSPIYS PEKRVLGQLH GGPSSCSATG ADRSDYYGRV FTSWTGGGTS
     ATRLSDWLDA AGTGAQFIDG LDSTGTPPV