ID G2G285_9FIRM Unreviewed; 506 AA.
AC G2G285;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 ORFNames=DOT_6126 {ECO:0000313|EMBL:EGW35888.1};
OS Desulfosporosinus sp. OT.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW35888.1, ECO:0000313|Proteomes:UP000004928};
RN [1] {ECO:0000313|EMBL:EGW35888.1, ECO:0000313|Proteomes:UP000004928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT {ECO:0000313|EMBL:EGW35888.1,
RC ECO:0000313|Proteomes:UP000004928};
RX PubMed=21994931; DOI=10.1128/JB.06018-11;
RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL J. Bacteriol. 193:6104-6105(2011).
CC -!- FUNCTION: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
CC {ECO:0000256|HAMAP-Rule:MF_01924}.
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:0000256|ARBA:ARBA00001362,
CC ECO:0000256|HAMAP-Rule:MF_01924};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01924};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01924};
CC -!- SIMILARITY: Belongs to the CapA family.
CC {ECO:0000256|ARBA:ARBA00005662}.
CC -!- SIMILARITY: Belongs to the peptidase M15D family. {ECO:0000256|HAMAP-
CC Rule:MF_01924}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGW35888.1}.
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DR EMBL; AGAF01000278; EGW35888.1; -; Genomic_DNA.
DR RefSeq; WP_009624778.1; NZ_AGAF01000278.1.
DR AlphaFoldDB; G2G285; -.
DR PATRIC; fig|913865.3.peg.5631; -.
DR eggNOG; COG2173; Bacteria.
DR eggNOG; COG2843; Bacteria.
DR OrthoDB; 9810906at2; -.
DR Proteomes; UP000004928; Unassembled WGS sequence.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd14840; D-Ala-D-Ala_dipeptidase_Aad; 1.
DR CDD; cd07381; MPP_CapA; 1.
DR Gene3D; 3.30.1380.10; -; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR HAMAP; MF_01924; A_A_dipeptidase; 1.
DR InterPro; IPR000755; A_A_dipeptidase.
DR InterPro; IPR019079; Capsule_synth_CapA.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR33393; POLYGLUTAMINE SYNTHESIS ACCESSORY PROTEIN RV0574C-RELATED; 1.
DR PANTHER; PTHR33393:SF11; POLYGLUTAMINE SYNTHESIS ACCESSORY PROTEIN RV0574C-RELATED; 1.
DR Pfam; PF01427; Peptidase_M15; 1.
DR Pfam; PF09587; PGA_cap; 1.
DR SMART; SM00854; PGA_cap; 1.
DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
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 Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|HAMAP-Rule:MF_01924}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..506
FT /note="D-alanyl-D-alanine dipeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003429821"
FT DOMAIN 217..455
FT /note="Capsule synthesis protein CapA"
FT /evidence="ECO:0000259|SMART:SM00854"
FT ACT_SITE 184
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT SITE 98
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
SQ SEQUENCE 506 AA; 56569 MW; 320A22CBE30A90A7 CRC64;
MFNRFLTILI TLTFIFGLTN QARADTQTSK KTDFVEIQQI IPSVMLDMKY ATTDNFTHTK
LYESSQALLR SGTAEKLKKV ADEVAKKGFR LKVWDAYRIP QAQFKMWKLV PDSRYVANPY
RGYSNHSRGS AIDLSLVDLA GNEIKMPTDF DNFTTAAART NANANAKYLG KIMVKHGFKP
LATEWWHFDD TNVYEPTETA KITSPSEPPK NERHEITLSA IGDVTLGQDD RFLYPGSFNQ
YFKQKGAGYF FSDVKKILSE DDLTIANLEG TLTEATEKPD KRFQGDKAFF FKGNPSYTAI
LKDGSIEAVD LANNHSMDYL DQGFRDTVTA LDKTGIKSFG YDKVAIYEKN ETKIGLIGVN
TLGKLEEGVN LINLEFDLAN KIQSLKDQTT LIVVSFHWGT ENISTPTSEQ RELGRLAVEQ
GASLVLGHHP HVLQPLEVYQ GKSIVYSLGN FVFGGNSNPS YKSTEIFQQT FSFENGNLVG
VNTPLIIPCE LSTSFRPVPL PQGANN
//