ID   VANX_ENTFA              Reviewed;         202 AA.
AC   Q47749;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=D-alanyl-D-alanine dipeptidase;
DE            Short=D-Ala-D-Ala dipeptidase;
DE            EC=3.4.13.22;
DE   AltName: Full=Vancomycin B-type resistance protein VanXB;
GN   Name=vanXB; Synonyms=vanX; OrderedLocusNames=EF_2293;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=8631706; DOI=10.1128/jb.178.5.1302-1309.1996;
RA   Evers S., Courvalin P.;
RT   "Regulation of VanB-type vancomycin resistance gene expression by the
RT   VanS(B)-VanR(B) two-component regulatory system in Enterococcus faecalis
RT   V583.";
RL   J. Bacteriol. 178:1302-1309(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
CC   -!- FUNCTION: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-alanyl-D-alanine + H2O = 2 D-alanine; Xref=Rhea:RHEA:20661,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57416, ChEBI:CHEBI:57822;
CC         EC=3.4.13.22;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- INDUCTION: By vancomycin, mediated by VanS/VanR.
CC       {ECO:0000269|PubMed:8631706}.
CC   -!- SIMILARITY: Belongs to the peptidase M15D family. {ECO:0000305}.
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DR   EMBL; U35369; AAB05628.1; -; Genomic_DNA.
DR   EMBL; AE016830; AAO82020.1; -; Genomic_DNA.
DR   RefSeq; NP_815950.1; NC_004668.1.
DR   RefSeq; WP_002368685.1; NZ_KE136528.1.
DR   AlphaFoldDB; Q47749; -.
DR   SMR; Q47749; -.
DR   STRING; 226185.EF_2293; -.
DR   MEROPS; M15.011; -.
DR   EnsemblBacteria; AAO82020; AAO82020; EF_2293.
DR   KEGG; efa:EF2293; -.
DR   PATRIC; fig|226185.45.peg.1239; -.
DR   eggNOG; COG2173; Bacteria.
DR   HOGENOM; CLU_060744_0_1_9; -.
DR   OMA; IRTEWWH; -.
DR   Proteomes; UP000001415; Chromosome.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1380.10; -; 1.
DR   HAMAP; MF_01924; A_A_dipeptidase; 1.
DR   InterPro; IPR000755; A_A_dipeptidase.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   Pfam; PF01427; Peptidase_M15; 1.
DR   PIRSF; PIRSF026671; AA_dipeptidase; 1.
DR   SUPFAM; SSF55166; SSF55166; 1.
PE   2: Evidence at transcript level;
KW   Antibiotic resistance; Cell wall biogenesis/degradation; Dipeptidase;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..202
FT                   /note="D-alanyl-D-alanine dipeptidase"
FT                   /id="PRO_0000217839"
FT   ACT_SITE        181
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   SITE            71
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        59
FT                   /note="A -> R (in Ref. 1; AAB05628)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   202 AA;  23224 MW;  532A0F4AC5D5606E CRC64;
     MENGFLFLDE MLHGVRWDAK YATWDNFTGK PVDGYEVNRI IGTKAVALAL REAQIHAAAL
     GYGLLLWDGY RPKSAVDCFL RWAAQPEDNL TKEKYYPNIE RAELITKGYV ASQSSHSRGS
     TIDLTLYHLD TGELVSMGSN FDFMDERSHH TAKGIGNAEA QNRRCLRKIM ESSGFQSYRF
     EWWHYKLIDE PYPDTYFNFA VS