(data stored in ACNUC1104 zone)

SWISSPROT: D3UZ17_XENBS

ID   D3UZ17_XENBS            Unreviewed;       243 AA.
AC   D3UZ17;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   13-FEB-2019, entry version 52.
DE   RecName: Full=D-alanyl-D-alanine dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924};
DE            Short=D-Ala-D-Ala dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924};
DE            EC=3.4.13.22 {ECO:0000256|HAMAP-Rule:MF_01924};
GN   Name=ddpX {ECO:0000256|HAMAP-Rule:MF_01924};
GN   OrderedLocusNames=XBJ1_0395 {ECO:0000313|EMBL:CBJ79545.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79545.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ79545.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79545.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Catalyzes hydrolysis of the D-alanyl-D-alanine
CC       dipeptide. {ECO:0000256|HAMAP-Rule:MF_01924}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-alanyl-D-alanine + H2O = 2 D-alanine;
CC         Xref=Rhea:RHEA:20661, ChEBI:CHEBI:15377, ChEBI:CHEBI:57416,
CC         ChEBI:CHEBI:57822; EC=3.4.13.22; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01924};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01924};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01924};
CC   -!- SIMILARITY: Belongs to the peptidase M15D family.
CC       {ECO:0000256|HAMAP-Rule:MF_01924}.
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; FN667741; CBJ79545.1; -; Genomic_DNA.
DR   STRING; 406818.XBJ1_0395; -.
DR   MEROPS; M15.011; -.
DR   EnsemblBacteria; CBJ79545; CBJ79545; XBJ1_0395.
DR   KEGG; xbo:XBJ1_0395; -.
DR   PATRIC; fig|406818.4.peg.365; -.
DR   eggNOG; ENOG4108WRV; Bacteria.
DR   eggNOG; COG2173; LUCA.
DR   HOGENOM; HOG000212010; -.
DR   KO; K08641; -.
DR   OMA; ETYSQNI; -.
DR   BioCyc; XBOV406818:XBJ1_RS01745-MONOMER; -.
DR   Proteomes; UP000002045; 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   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   SUPFAM; SSF55166; SSF55166; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UZ17.
DR   SWISS-2DPAGE; D3UZ17.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01924};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01924};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_01924};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01924};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   ACT_SITE    213    213       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   METAL       144    144       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   METAL       151    151       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01924}.
FT   METAL       216    216       Zinc; via pros nitrogen; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   SITE         95     95       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
SQ   SEQUENCE   243 AA;  27725 MW;  D1FE3F30699C8D42 CRC64;
     MFLSIAMENN TVDKIAVEKL FDWEVINGMP INECHEPLEI ITDTDKLRQQ SAYFFAGIKG
     SIEYCTVREN VARKLVIASQ LLPPHLGLLV LDGWRSRETQ QALQEQTQIK IADQYRHLSV
     EEQKALLQQF VAPAPTEQHQ ISPHLTGGSV DVTLFDVASG KPLFLGTEFD EVTELSYTAA
     LEKEPEKNMP AILYRRLLYN AMIQVGFTNL PTEWWHYDYG NSLWAFYKND IAIYGAVDGT
     RNR
//

If you have problems or comments...

PBIL Back to PBIL home page