ID   LSTP_STAST              Reviewed;         480 AA.
AC   P10548;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Lysostaphin;
DE            EC=3.4.24.75;
DE   AltName: Full=Glycyl-glycine endopeptidase;
DE   Flags: Precursor;
GN   Name=lss;
OS   Staphylococcus staphylolyticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2828883; DOI=10.1007/bf00331163;
RA   Heinrich P., Rosenstein R., Boehmer M., Sonner P., Goetz F.;
RT   "The molecular organization of the lysostaphin gene and its sequences
RT   repeated in tandem.";
RL   Mol. Gen. Genet. 209:563-569(1987).
CC   -!- FUNCTION: Lyses staphylococcal cells by hydrolyzing the polyglycine
CC       interpeptide bridges of the peptidoglycan.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-
CC         peptide link joining staphylococcal cell wall peptidoglycans.;
CC         EC=3.4.24.75;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase M23B 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   EMBL; X06121; CAA29494.1; -; Genomic_DNA.
DR   PIR; S01079; S01079.
DR   AlphaFoldDB; P10548; -.
DR   SMR; P10548; -.
DR   MEROPS; M23.004; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.70.10; -; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR016047; Peptidase_M23.
DR   InterPro; IPR003646; SH3-like_bac-type.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   Pfam; PF08460; SH3_5; 1.
DR   SMART; SM00287; SH3b; 1.
DR   SUPFAM; SSF51261; SSF51261; 1.
DR   PROSITE; PS51781; SH3B; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Repeat; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..234
FT                   /id="PRO_0000026817"
FT   CHAIN           235..480
FT                   /note="Lysostaphin"
FT                   /id="PRO_0000026818"
FT   REPEAT          49..61
FT                   /note="1"
FT   REPEAT          62..74
FT                   /note="2"
FT   REPEAT          75..87
FT                   /note="3"
FT   REPEAT          88..100
FT                   /note="4"
FT   REPEAT          101..113
FT                   /note="5"
FT   REPEAT          114..126
FT                   /note="6"
FT   REPEAT          127..139
FT                   /note="7"
FT   REPEAT          140..152
FT                   /note="8"
FT   REPEAT          153..165
FT                   /note="9"
FT   REPEAT          166..178
FT                   /note="10"
FT   REPEAT          179..191
FT                   /note="11"
FT   REPEAT          192..204
FT                   /note="12"
FT   REPEAT          205..217
FT                   /note="13"
FT   REPEAT          218..230
FT                   /note="14; approximate"
FT   DOMAIN          400..468
FT                   /note="SH3b"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT   REGION          49..230
FT                   /note="14 X 13 AA tandem repeats of A-E-V-E-T-S-K-[AP]-P-V-
FT                   E-N-T"
FT   REGION          51..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        347
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   480 AA;  51687 MW;  62A071A0D248891D CRC64;
     MKKTKNNYYT TPLAIGLSTF ALASIVYGGI QNETHASEKS NMDVSKKVAE VETSKPPVEN
     TAEVETSKAP VENTAEVETS KAPVENTAEV ETSKAPVENT AEVETSKAPV ENTAEVETSK
     APVENTAEVE TSKAPVENTA EVETSKAPVE NTAEVETSKA PVENTAEVET SKAPVENTAE
     VETSKAPVEN TAEVETSKAP VENTAEVETS KAPVENTAEV ETSKALVQNR TALRAATHEH
     SAQWLNNYKK GYGYGPYPLG INGGIHYGVD FFMNIGTPVK AISSGKIVEA GWSNYGGGNQ
     IGLIENDGVH RQWYMHLSKY NVKVGDYVKA GQIIGWSGST GYSTAPHLHF QRMVNSFSNS
     TAQDPMPFLK SAGYGKAGGT VTPTPNTGWK TNKYGTLYKS ESASFTPNTD IITRTTGPFR
     SMPQSGVLKA GQTIHYDEVM KQDGHVWVGY TGNSGQRIYL PVRTWNKSTN TLGVLWGTIK