LSTP_STASI
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 03-AUG-2022, entry version 116.
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; Firmicutes; 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}.
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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 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 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 COMPBIAS 66..232
FT /note="Polar residues"
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 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
