VANX_STRCO
ID VANX_STRCO Reviewed; 202 AA.
AC Q9XAK6;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=D-alanyl-D-alanine dipeptidase {ECO:0000255|HAMAP-Rule:MF_01924};
DE Short=D-Ala-D-Ala dipeptidase {ECO:0000255|HAMAP-Rule:MF_01924};
DE EC=3.4.13.22 {ECO:0000255|HAMAP-Rule:MF_01924};
GN Name=vanX; OrderedLocusNames=SCO3596; ORFNames=SC66T3.07;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=11881895; DOI=10.1016/s0923-2508(01)01282-7;
RA Tan A.L., Loke P., Sim T.-S.;
RT "Molecular cloning and functional characterisation of VanX, a D-alanyl-D-
RT alanine dipeptidase from Streptomyces coelicolor A3(2).";
RL Res. Microbiol. 153:27-32(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. May
CC play a role in immunity or defense against glycopeptide antibiotics
CC (perhaps at a moderate level) in the soil environment. Might confer
CC vancomycin resistance to S.coelicolor. {ECO:0000255|HAMAP-
CC Rule:MF_01924, ECO:0000269|PubMed:11881895}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_01924,
CC ECO:0000269|PubMed:11881895};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01924};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01924};
CC -!- SIMILARITY: Belongs to the peptidase M15D family. {ECO:0000255|HAMAP-
CC Rule:MF_01924}.
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DR EMBL; AF367376; AAK52963.1; -; Genomic_DNA.
DR EMBL; AL939117; CAB45463.1; -; Genomic_DNA.
DR PIR; T35364; T35364.
DR RefSeq; NP_627791.1; NC_003888.3.
DR RefSeq; WP_011029111.1; NZ_VNID01000003.1.
DR AlphaFoldDB; Q9XAK6; -.
DR SMR; Q9XAK6; -.
DR STRING; 100226.SCO3596; -.
DR MEROPS; M15.011; -.
DR GeneID; 1099032; -.
DR KEGG; sco:SCO3596; -.
DR PATRIC; fig|100226.15.peg.3653; -.
DR eggNOG; COG2173; Bacteria.
DR HOGENOM; CLU_060744_0_1_11; -.
DR InParanoid; Q9XAK6; -.
DR OMA; GGDHDLM; -.
DR PhylomeDB; Q9XAK6; -.
DR BRENDA; 3.4.13.22; 5998.
DR Proteomes; UP000001973; 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 1: Evidence at protein 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_0000217841"
FT ACT_SITE 181
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01924"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01924"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01924"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01924"
FT SITE 71
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01924"
SQ SEQUENCE 202 AA; 22710 MW; 0CDAAA78C2D07D3F CRC64;
MTGDFAFVDE LVSGIRWDAK YATWDNFTGK PVDGYLANRI VGTKALCAAL GRAQERAEDL
GFGLLLWDGY RPQRAVDCFL RWSQQPEDGR TKARHYPNIG RAEMFDRGYV AARSGHSRGA
TVDLTLYHLT TGELAAMGGG HDLMDPISHH DARDVPRAEA ANRRHLRSIM AACGFASYAC
EWWHYTLKEE PHPDTYFDFP IA
