(data stored in ACNUC1104 zone)

SWISSPROT: D5US96_TSUPD

ID   D5US96_TSUPD            Unreviewed;       210 AA.
AC   D5US96;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   13-FEB-2019, entry version 48.
DE   RecName: Full=D-alanyl-D-alanine dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924, ECO:0000256|PIRNR:PIRNR026671};
DE            Short=D-Ala-D-Ala dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924, ECO:0000256|PIRNR:PIRNR026671};
DE            EC=3.4.13.22 {ECO:0000256|HAMAP-Rule:MF_01924, ECO:0000256|PIRNR:PIRNR026671};
GN   OrderedLocusNames=Tpau_0522 {ECO:0000313|EMBL:ADG77163.1};
OS   Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 /
OS   NBRC 16120 / NCTC 13040) (Corynebacterium paurometabolum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG77163.1, ECO:0000313|Proteomes:UP000001213};
RN   [1] {ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C.,
RA   Tapia R., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG77163.1, ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RX   PubMed=21886861;
RA   Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA   Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Tapia R., Han C., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Yasawong M., Brambilla E.M., Rohde M.,
RA   Sikorski J., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Tsukamurella paurometabola type strain
RT   (no. 33).";
RL   Stand. Genomic Sci. 4:342-351(2011).
CC   -!- FUNCTION: Catalyzes hydrolysis of the D-alanyl-D-alanine
CC       dipeptide. {ECO:0000256|HAMAP-Rule:MF_01924,
CC       ECO:0000256|PIRNR:PIRNR026671}.
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, ECO:0000256|PIRNR:PIRNR026671};
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, ECO:0000256|PIRNR:PIRNR026671}.
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DR   EMBL; CP001966; ADG77163.1; -; Genomic_DNA.
DR   RefSeq; WP_013125205.1; NC_014158.1.
DR   STRING; 521096.Tpau_0522; -.
DR   MEROPS; M15.011; -.
DR   EnsemblBacteria; ADG77163; ADG77163; Tpau_0522.
DR   KEGG; tpr:Tpau_0522; -.
DR   eggNOG; ENOG4108UQS; Bacteria.
DR   eggNOG; COG2173; LUCA.
DR   HOGENOM; HOG000200848; -.
DR   KO; K08641; -.
DR   OMA; GGDHDLM; -.
DR   OrthoDB; 880710at2; -.
DR   BioCyc; TPAU521096:G1GKO-505-MONOMER; -.
DR   Proteomes; UP000001213; 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   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   3: Inferred from homology;
DR   PRODOM; D5US96.
DR   SWISS-2DPAGE; D5US96.
KW   Cell wall biogenesis/degradation {ECO:0000256|PIRNR:PIRNR026671};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001213};
KW   Dipeptidase {ECO:0000256|HAMAP-Rule:MF_01924,
KW   ECO:0000256|PIRNR:PIRNR026671, ECO:0000313|EMBL:ADG77163.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01924,
KW   ECO:0000256|PIRNR:PIRNR026671, ECO:0000313|EMBL:ADG77163.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01924};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_01924,
KW   ECO:0000256|PIRNR:PIRNR026671};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01924,
KW   ECO:0000256|PIRNR:PIRNR026671};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001213};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   ACT_SITE    181    181       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   METAL       116    116       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   METAL       123    123       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01924}.
FT   METAL       184    184       Zinc; via pros nitrogen; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
FT   SITE         71     71       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01924}.
SQ   SEQUENCE   210 AA;  23626 MW;  8E9D11767E51B57C CRC64;
     MNTDFVYVDE HVPGVRWDAK YATWDNFTGK PVDGYLANRI VGTRVLCAGL RLAQRHAATL
     GYGLLLWDGY RPQRAVDRFV AWSRQPENGR TKQRHYPNIA RADMFELGYV ATRSGHSRGS
     TVDLTLYHLD SGDLADMGGD HDLMDPVSHH GAPGIGEPAA RNRARLATIM EDAGFLRYDS
     EWWHYTLHDE PFPTTYFDFP ITLAAGSRAA
//

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