ALE1_STACP
ID ALE1_STACP Reviewed; 362 AA.
AC O05156;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Glycyl-glycine endopeptidase ALE-1;
DE EC=3.4.24.75;
DE AltName: Full=Staphylolytic enzyme ALE-1;
DE Flags: Precursor;
OS Staphylococcus capitis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=29388;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=EPK1;
RX PubMed=9023202; DOI=10.1128/jb.179.4.1193-1202.1997;
RA Sugai M., Fujiwara T., Akiyama T., Ohara M., Komatsuzawa H., Inoue S.,
RA Suginaka H.;
RT "Purification and molecular characterization of glycylglycine endopeptidase
RT produced by Staphylococcus capitis EPK1.";
RL J. Bacteriol. 179:1193-1202(1997).
RN [2]
RP MUTAGENESIS OF HIS-150; ASP-154; HIS-200; HIS-231 AND HIS-233.
RX PubMed=15629919; DOI=10.1128/jb.187.2.480-487.2005;
RA Fujiwara T., Aoki S., Komatsuzawa H., Nishida T., Ohara M., Suginaka H.,
RA Sugai M.;
RT "Mutation analysis of the histidine residues in the glycylglycine
RT endopeptidase ALE-1.";
RL J. Bacteriol. 187:480-487(2005).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-9.;
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; D86328; BAA13069.1; -; Genomic_DNA.
DR PDB; 1R77; X-ray; 1.75 A; A/B=271-362.
DR PDBsum; 1R77; -.
DR AlphaFoldDB; O05156; -.
DR SMR; O05156; -.
DR MEROPS; M23.012; -.
DR EvolutionaryTrace; O05156; -.
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.
FT SIGNAL 1..35
FT CHAIN 36..362
FT /note="Glycyl-glycine endopeptidase ALE-1"
FT /id="PRO_0000026814"
FT DOMAIN 282..350
FT /note="SH3b"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT REGION 35..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 231
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT STRAND 279..291
FT /evidence="ECO:0007829|PDB:1R77"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:1R77"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:1R77"
FT STRAND 315..324
FT /evidence="ECO:0007829|PDB:1R77"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:1R77"
FT STRAND 339..347
FT /evidence="ECO:0007829|PDB:1R77"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:1R77"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:1R77"
SQ SEQUENCE 362 AA; 39350 MW; C50DCDFDF9F6400E CRC64;
MDTNRKFTLV KSLSIGLGTF LVGSVFLTVN DEASASTKVD APKVEQEAPA KADAPKVEQE
APAKADAPKV EQEAPAKVDA PKVEQEAPAK VDAPKVEQEA PAKADAPKVE QKRTFVREAA
QSNHSASWLN NYKKGYGYGP YPLGINGGNH YGVDFFMNVG TPVRAISDGK IVEAGWTNYG
GGNEIGLVEN DGVHRQWYMH LSKFNVKVGD RVKAGQIIGW SGSTGYSTAP HLHFQRMTNS
FSNNTAQDPM PFLKSAGYGS NSTSSSNNNG YKTNKYGTLY KSESASFTAN TDIITRLTGP
FRSMPQSGVL RKGLTIKYDE VMKQDGHVWV GYNTNSGKRV YLPVRTWNES TGELGPLWGT
IK
