ID A0A143X5D6_9FIRM Unreviewed; 346 AA.
AC A0A143X5D6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Putative aminopeptidase YsdC {ECO:0000313|EMBL:CVH77818.1};
DE EC=3.4.11.- {ECO:0000313|EMBL:CVH77818.1};
GN Name=ysdC_2 {ECO:0000313|EMBL:CVH77818.1};
GN ORFNames=BN3662_02418 {ECO:0000313|EMBL:CVH77818.1};
OS Clostridiales bacterium CHKCI006.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1780379 {ECO:0000313|EMBL:CVH77818.1, ECO:0000313|Proteomes:UP000198633};
RN [1] {ECO:0000313|EMBL:CVH77818.1, ECO:0000313|Proteomes:UP000198633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHKC6 {ECO:0000313|EMBL:CVH77818.1};
RA Oliw E.H.;
RL Submitted (JAN-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; FCNA01000129; CVH77818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143X5D6; -.
DR STRING; 1780379.BN3662_02418; -.
DR OrthoDB; 361940at2; -.
DR Proteomes; UP000198633; 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; cd05657; M42_glucanase_like; 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:SF7; AMINOPEPTIDASE YHFE-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:CVH77818.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CVH77818.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000198633}.
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 346 AA; 38504 MW; 57F3A5EE9273E3D6 CRC64;
MEFQFKQDVV ATLIQELMAI DSPSGYTQNA IAYIENKANA YQLPFMRTHK GNGIIYMPGR
NAKTTIGVCA HVDTLGLMVR SIKSNGRLCF TKVGGPILPS LDSEWCKVYT REGKVYSGTI
YSTSPAAHVF KDAASKERTE DTMEVILDEK VKSKEEVEKL GIQTGDYICF DPKTTITENG
FIKSRFLDDK LSVAIILGII DFMVENHIQP ENNVKFMFST YEEVGHGMAY IPEDITELLC
VDMGCIGQDL NCSEYDVSIC AKDSSGPYDY QMTGDLIALA KKHQLQYAVD IYPYYGSDAS
AALRAGHDIR AALIGPGVFA SHGYERSTME AVDQSMQLVY YYLTNQ
//
