ID A0A1Y4DD33_9BACT Unreviewed; 383 AA.
AC A0A1Y4DD33;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=B5F75_04890 {ECO:0000313|EMBL:OUO56532.1};
OS Elusimicrobium sp. An273.
OC Bacteria; Elusimicrobiota; Elusimicrobia; Elusimicrobiales;
OC Elusimicrobiaceae; Elusimicrobium.
OX NCBI_TaxID=1965617 {ECO:0000313|EMBL:OUO56532.1, ECO:0000313|Proteomes:UP000196368};
RN [1] {ECO:0000313|Proteomes:UP000196368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An273 {ECO:0000313|Proteomes:UP000196368};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR001123-2};
CC -!- SIMILARITY: Belongs to the peptidase M42 family.
CC {ECO:0000256|PIRNR:PIRNR001123}.
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:OUO56532.1}.
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DR EMBL; NFJD01000003; OUO56532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4DD33; -.
DR OrthoDB; 9776600at2; -.
DR Proteomes; UP000196368; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR010162; PepT-like.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR008007; Peptidase_M42.
DR NCBIfam; TIGR01883; PepT-like; 1.
DR PANTHER; PTHR42994; PEPTIDASE T; 1.
DR PANTHER; PTHR42994:SF2; T, PUTATIVE-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF001123; PepA_GA; 3.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000196368}.
FT DOMAIN 185..275
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 383 AA; 41653 MW; 5945F1AAE2D09C95 CRC64;
MMKLNQQRLI DTFLELVQID SESFHEKKIH GFLVSRLKEL GCRVYVDKAG SAYNTDAPGN
IIAFLPGTAK SKPVVLCSHM DTVVPGKGVK PVVKKDCITS DGTTILGADD KAGLAIILEV
LRTLKEQTQV PYPPVEAVFT LTEETGMQGA KNLDYKKIKG REGLILDNEE VTELLVQGPA
VNTIEVWIKG LASHAGVCPE KGISALEVAA YALSQMKLGR VDKETVANFG VVQGGKVTNV
VMDEVYLKGE ARSLSDAKLA KQTAHMKACF EKAVKHFTKK IDGKVHKPQV KFVPFKRYPA
VNVPRNNEMV KDILSAAKKL GVRVRAAASG GGCDANVLSG FGFTLPNLGV GCRNCHTLKE
KLILKEFFQA FEITLAAVLA YRK
//
