ID A0A1G4FGC7_9FIRM Unreviewed; 351 AA.
AC A0A1G4FGC7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Putative aminopeptidase YsdC {ECO:0000313|EMBL:SCL82607.1};
DE EC=3.4.11.- {ECO:0000313|EMBL:SCL82607.1};
GN Name=ysdC_3 {ECO:0000313|EMBL:SCL82607.1};
GN ORFNames=PP176A_0296 {ECO:0000313|EMBL:SCL82607.1};
OS Sporanaerobacter sp. PP17-6a.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Sporanaerobacteraceae;
OC Sporanaerobacter.
OX NCBI_TaxID=1891289 {ECO:0000313|EMBL:SCL82607.1, ECO:0000313|Proteomes:UP000179042};
RN [1] {ECO:0000313|EMBL:SCL82607.1, ECO:0000313|Proteomes:UP000179042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP176A {ECO:0000313|EMBL:SCL82607.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
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DR EMBL; FMIF01000002; SCL82607.1; -; Genomic_DNA.
DR RefSeq; WP_071138667.1; NZ_FMIF01000002.1.
DR AlphaFoldDB; A0A1G4FGC7; -.
DR Proteomes; UP000179042; 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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05656; M42_Frv; 1.
DR Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF0; AMINOPEPTIDASE YPDE-RELATED; 1.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:SCL82607.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SCL82607.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000179042}.
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 351 AA; 38690 MW; 562B377ECB0EF8BC CRC64;
MESTEFLERL SNGFGPSGYE YSLKDSIADV MGKYADELKV DNLGNIIAIK RGNKKESKIK
IMVAAHMDEI GLMVTAIEDN GFLRFTQIGG IDQRTLLGQE VIVHGEKDLF GVIGVKPPHL
QTRDELDKAV KMEDMAIDIG YSKEEVEKIV KIGDVITIRR KLTHLLNEKY TGKALDDRTG
IIALYECIKE LKKLNHEADA YLVSTVQEEV GTRGAYTSTY GINPDIGIAV DVGFASSPEI
PKEYTLDIGK GPGITIGGNI HPGLRKKLVE IAKEYNIPYQ FEVEPGPTGT DARAIQISRE
GIPALCISLP LKYMHTSVEV IDMNDIKNTG KLLALFIASI SKENLEGLLC Y
//
