ID A0A1K1N293_SELRU Unreviewed; 457 AA.
AC A0A1K1N293;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN02910323_1036 {ECO:0000313|EMBL:SFW28422.1};
OS Selenomonas ruminantium.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=971 {ECO:0000313|EMBL:SFW28422.1, ECO:0000313|Proteomes:UP000182958};
RN [1] {ECO:0000313|Proteomes:UP000182958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3 {ECO:0000313|Proteomes:UP000182958};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the peptidase M15D family. {ECO:0000256|HAMAP-
CC Rule:MF_01924}.
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DR EMBL; FPJA01000005; SFW28422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1K1N293; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000182958; 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:0016740; F:transferase 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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd14817; D-Ala-D-Ala_dipeptidase_VanX; 1.
DR CDD; cd16913; YkuD_like; 1.
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 InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR43126; D-ALANYL-D-ALANINE DIPEPTIDASE; 1.
DR PANTHER; PTHR43126:SF1; D-ALANYL-D-ALANINE DIPEPTIDASE; 1.
DR Pfam; PF01427; Peptidase_M15; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 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:UP000182958};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01924}.
FT DOMAIN 295..447
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT ACT_SITE 222
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
FT SITE 111
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01924"
SQ SEQUENCE 457 AA; 51295 MW; 38B881916A9EC0DA CRC64;
MFFGKGSFFR GLMLPLLIFS LLFGSLPTVL AAPQSKVNPH DSSGFVVLSD VVPDIIQEIR
YYSTYNFVGD RIDGYNEPIA LMTKEAAQAL KAVSDDVKAQ GYRLKIYDAY RPQRAVTNFV
KWAENLKDKR MKDYFYPEVE KNRLFAEGYI AAKSGHSRGS TVDLTLFDMS TGKELDMGGT
FDYFGLLSHP DYRGKLTEKQ IKNRMILREA MLRHGFKPLE EEWWHFTLKD EPYPDTYFEF
PVQRLPESNL VTKASPAWVT NLPAAKTAKQ LFVVGAVSGT TAWVSLHEKD ANGKWQQIMT
TPGFIGKNGL GKEKEGDNKT PVGTFRFTAA FGIAPNPGSI MPYKQVDENF YWSGDARPGM
KYNEMVDIRQ LPGLDKDGSE HLVDYNPHYI YCLNIGYNEA GTPGKGSAIF LHCLGSNKPY
TGGCVAIPED KMRFVLQHVR PECKVVIDSL TNLGGSL
//
