ID A0A1L6J8E8_9SPHN Unreviewed; 767 AA.
AC A0A1L6J8E8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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 ORFNames=BRX40_06840 {ECO:0000313|EMBL:APR52188.1};
OS Sphingomonas koreensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=93064 {ECO:0000313|EMBL:APR52188.1, ECO:0000313|Proteomes:UP000185161};
RN [1] {ECO:0000313|Proteomes:UP000185161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ABOJV {ECO:0000313|Proteomes:UP000185161};
RA Conlan S., Thomas P.J., Mullikin J., Palmore T.N., Frank K.M., Segre J.A.;
RT "Whole genome sequencing of Sphingomonas sp. ABOJV.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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 beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00038473}.
CC -!- SIMILARITY: Belongs to the peptidase M15D family. {ECO:0000256|HAMAP-
CC Rule:MF_01924}.
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DR EMBL; CP018820; APR52188.1; -; Genomic_DNA.
DR RefSeq; WP_075151092.1; NZ_QQZI01000001.1.
DR AlphaFoldDB; A0A1L6J8E8; -.
DR STRING; 93064.BRX40_06840; -.
DR GeneID; 67168672; -.
DR KEGG; skr:BRX40_06840; -.
DR Proteomes; UP000185161; 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 CDD; cd14840; D-Ala-D-Ala_dipeptidase_Aad; 1.
DR Gene3D; 3.30.1380.10; -; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR HAMAP; MF_01924; A_A_dipeptidase; 1.
DR InterPro; IPR000755; A_A_dipeptidase.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR PANTHER; PTHR22935:SF95; BETA-LACTAMASE-LIKE 1-RELATED; 1.
DR PANTHER; PTHR22935; PENICILLIN-BINDING PROTEIN; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR Pfam; PF01427; Peptidase_M15; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000185161};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|HAMAP-Rule:MF_01924}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..767
FT /note="D-alanyl-D-alanine dipeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012973278"
FT DOMAIN 30..350
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
FT ACT_SITE 743
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT BINDING 678
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT BINDING 685
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT BINDING 746
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT SITE 649
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
SQ SEQUENCE 767 AA; 83207 MW; DCE735FF7B889671 CRC64;
MRAMLAAAVV CAAPAAAQPA ELAAVTRSVE AAAQAELADK EIPSIAVALV DRSGVVWSRA
WGHADADGKV PATPATLYRA GSVSKLFTDI AVMRLVEQGK LDLDAPVTRY LPDFRPQNPF
GGAITLRQLM THRSGLVREA PRGHYFDSDA KGQADAVASL NATRLVAAPG AITKYSNAGI
AVVGEVVARV SGKPYAQAVA DLVLRPLGMG ASAFERSALK GPVAYSQMNS FDGGRWPAPP
LELGTPAAGS LYTDTADLGA FARAMLNGGG AVLKPATLAE MWREQYGKTG TRSFGLGFGL
GTLDGQRTVG HGGAVYGHVA SLQLMPDAGI GVVVFATVDA GNAAQRIGAH ALRNWLAARE
GRALPGWQRS NAISGDEAIR LSGRFENGGD SVNLRVFDGR LVLDAPELAG ELRRIGDRYV
LDDAQLWRDG VAVAPDASWV ELDGRRFTRA QWRRPPPPNA ELAALIGEYG WDYNVLRIYE
RDGKPYVRVE WVDWLPLTRI AADHYAFPKD HGLYPLEALT FERDAAGKVT AAKLGAIRFP
RRDFGAEGEA AIRKVMATGG IDTVREGARR ATPPVEVEPK VKSDLVAVQS LDPAIRLDIR
YAGTNNFLGQ QIYERPGAFL QRPAAEAMAR INRSLAPQGF GLLVHDAYRP WYVTKMFWDA
TPPASRIFVA DPSKGSRHNR GAAVDLTMVD LATGKPMITT GRYDEMSSRS YTNYVGGSDE
QRWLREVLRR AMEADGFTVY PQEWWHFDRD GWQQYPIGNR SFEELEK
//