ID LSTP_STASI Reviewed; 493 AA. AC P10547; O05988; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 10-JUN-2026, entry version 127. DE RecName: Full=Lysostaphin; DE EC=3.4.24.75; DE AltName: Full=Glycyl-glycine endopeptidase; DE Flags: Precursor; GN Name=lss; OS Staphylococcus simulans. OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1286; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DSM 20723 / NRRL B-2628; RX PubMed=3547405; DOI=10.1073/pnas.84.5.1127; RA Recsei P.A., Gruss A.D., Novick R.P.; RT "Cloning, sequence, and expression of the lysostaphin gene from RT Staphylococcus simulans."; RL Proc. Natl. Acad. Sci. U.S.A. 84:1127-1131(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 1362; RX PubMed=9106216; DOI=10.1046/j.1365-2958.1997.2911657.x; RA Thumm G., Goetz F.; RT "Studies on prolysostaphin processing and characterization of the RT lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar RT staphylolyticus."; RL Mol. Microbiol. 23:1251-1265(1997). 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; CC Note=Binds 1 zinc ion per subunit.; 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; U66883; AAB53783.1; -; Genomic_DNA. DR EMBL; M15686; AAA26655.1; -; Genomic_DNA. DR PIR; A25881; A25881. DR PDB; 4LXC; X-ray; 3.50 A; A/B/C/D=248-493. DR PDB; 4QP5; X-ray; 1.26 A; A/B=248-386. DR PDB; 4QPB; X-ray; 1.78 A; A/B=248-386. DR PDB; 5LEO; X-ray; 1.60 A; A/B=401-493. DR PDB; 5NMY; NMR; -; A=251-493. DR PDB; 6RJE; X-ray; 2.50 A; A=401-493. DR PDB; 6RK4; X-ray; 1.43 A; A=1-493. DR PDBsum; 4LXC; -. DR PDBsum; 4QP5; -. DR PDBsum; 4QPB; -. DR PDBsum; 5LEO; -. DR PDBsum; 5NMY; -. DR PDBsum; 6RJE; -. DR PDBsum; 6RK4; -. DR AlphaFoldDB; P10547; -. DR SMR; P10547; -. DR MEROPS; M23.004; -. DR KEGG; ag:AAA26655; -. DR KEGG; ag:AAB53783; -. DR BRENDA; 3.4.24.75; 5881. DR EvolutionaryTrace; P10547; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:TreeGrafter. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd12797; M23_peptidase; 1. DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR050570; Cell_wall_metabolism_enzyme. DR InterPro; IPR011055; Dup_hybrid_motif. DR InterPro; IPR058241; Lysostaphin_N. DR InterPro; IPR016047; M23ase_b-sheet_dom. DR InterPro; IPR003646; SH3-like_bac-type. DR PANTHER; PTHR21666:SF270; MUREIN HYDROLASE ACTIVATOR ENVC; 1. DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1. DR Pfam; PF25533; Lysostaphin_N; 1. DR Pfam; PF01551; Peptidase_M23; 1. DR Pfam; PF08460; SH3_5; 1. DR SMART; SM00287; SH3b; 1. DR SUPFAM; SSF51261; Duplicated hybrid motif; 1. DR PROSITE; PS51781; SH3B; 1. PE 1: Evidence at protein level; KW 3D-structure; 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..247 FT /id="PRO_0000026815" FT CHAIN 248..493 FT /note="Lysostaphin" FT /id="PRO_0000026816" 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" FT REPEAT 231..243 FT /note="15; approximate" FT DOMAIN 413..481 FT /note="SH3b" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01117" FT REGION 49..243 FT /note="15 X 13 AA approximate tandem repeats of A-E-V-E-T- FT S-K-A-P-V-E-N-T" FT REGION 52..232 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 360 FT BINDING 279 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 283 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 362 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT CONFLICT 135..238 FT /note="Missing (in Ref. 1)" FT /evidence="ECO:0000305" FT STRAND 251..253 FT /evidence="ECO:0007829|PDB:4LXC" FT HELIX 256..260 FT /evidence="ECO:0007829|PDB:4QP5" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:5NMY" FT STRAND 267..269 FT /evidence="ECO:0007829|PDB:4QP5" FT STRAND 271..273 FT /evidence="ECO:0007829|PDB:4QP5" FT HELIX 274..276 FT /evidence="ECO:0007829|PDB:4QP5" FT STRAND 281..285 FT /evidence="ECO:0007829|PDB:4QP5" FT STRAND 291..293 FT /evidence="ECO:0007829|PDB:4QP5" FT STRAND 298..306 FT /evidence="ECO:0007829|PDB:4QP5" FT TURN 307..310 FT /evidence="ECO:0007829|PDB:4QP5" FT STRAND 311..318 FT /evidence="ECO:0007829|PDB:4QP5" FT STRAND 321..334 FT /evidence="ECO:0007829|PDB:4QP5" FT STRAND 346..349 FT /evidence="ECO:0007829|PDB:4QP5" FT STRAND 353..355 FT /evidence="ECO:0007829|PDB:5NMY" FT STRAND 360..372 FT /evidence="ECO:0007829|PDB:4QP5" FT HELIX 379..383 FT /evidence="ECO:0007829|PDB:4QP5" FT TURN 385..388 FT /evidence="ECO:0007829|PDB:4LXC" FT STRAND 389..391 FT /evidence="ECO:0007829|PDB:4LXC" FT STRAND 399..401 FT /evidence="ECO:0007829|PDB:4LXC" FT STRAND 410..422 FT /evidence="ECO:0007829|PDB:6RK4" FT STRAND 424..431 FT /evidence="ECO:0007829|PDB:6RK4" FT STRAND 437..441 FT /evidence="ECO:0007829|PDB:6RK4" FT STRAND 447..455 FT /evidence="ECO:0007829|PDB:6RK4" FT STRAND 458..464 FT /evidence="ECO:0007829|PDB:6RK4" FT STRAND 468..479 FT /evidence="ECO:0007829|PDB:6RK4" FT TURN 480..483 FT /evidence="ECO:0007829|PDB:6RK4" FT HELIX 486..488 FT /evidence="ECO:0007829|PDB:6RK4" FT STRAND 489..492 FT /evidence="ECO:0007829|PDB:6RK4" SQ SEQUENCE 493 AA; 53091 MW; 2BFA751D47865A1A CRC64; MKKTKNNYYT RPLAIGLSTF ALASIVYGGI QNETHASEKS NMDVSKKVAE VETSKAPVEN TAEVETSKAP VENTAEVETS KAPVENTAEV ETSKAPVENT AEVETSKAPV ENTAEVETSK APVENTAEVE TSKAPVENTA EVETSKAPVE NTAEVETSKA PVENTAEVET SKAPVENTAE VETSKAPVEN TAEVETSKAP VENTAEVETS KAPVENTAEV ETSKAPVENT AEVETSKALV QNRTALRAAT HEHSAQWLNN YKKGYGYGPY PLGINGGMHY GVDFFMNIGT PVKAISSGKI VEAGWSNYGG GNQIGLIEND GVHRQWYMHL SKYNVKVGDY VKAGQIIGWS GSTGYSTAPH LHFQRMVNSF SNSTAQDPMP FLKSAGYGKA GGTVTPTPNT GWKTNKYGTL YKSESASFTP NTDIITRTTG PFRSMPQSGV LKAGQTIHYD EVMKQDGHVW VGYTGNSGQR IYLPVRTWNK STNTLGVLWG TIK //