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 27-MAR-2024, entry version 107.
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; Bacillota; 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}.
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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 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; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR046567; Lysostaphin_N.
DR InterPro; IPR016047; Peptidase_M23.
DR InterPro; IPR003646; SH3-like_bac-type.
DR PANTHER; PTHR21666:SF270; OUTER MEMBRANE ANTIGENIC LIPOPROTEIN B; 1.
DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR Pfam; PF20481; DUF6721; 2.
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 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
//
