ID A0A174KD02_9CLOT Unreviewed; 359 AA.
AC A0A174KD02;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Cellulase M and related proteins {ECO:0000313|EMBL:CUP07129.1};
DE EC=3.4.11.- {ECO:0000313|EMBL:CUP07129.1};
GN Name=ysdC_5 {ECO:0000313|EMBL:CUP07129.1};
GN ORFNames=ERS852471_02929 {ECO:0000313|EMBL:CUP07129.1};
OS Clostridium disporicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84024 {ECO:0000313|EMBL:CUP07129.1, ECO:0000313|Proteomes:UP000095594};
RN [1] {ECO:0000313|EMBL:CUP07129.1, ECO:0000313|Proteomes:UP000095594}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5834856 {ECO:0000313|EMBL:CUP07129.1,
RC ECO:0000313|Proteomes:UP000095594};
RG Pathogen Informatics;
RL Submitted (SEP-2015) 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; CYZX01000025; CUP07129.1; -; Genomic_DNA.
DR RefSeq; WP_055267807.1; NZ_CYZX01000025.1.
DR AlphaFoldDB; A0A174KD02; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000095594; 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 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:CUP07129.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CUP07129.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000095594}.
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 359 AA; 39320 MW; B0239BE00D0CBBBC CRC64;
MINLNVLKEL SDAFGPSGFE DDVVEVIKKH CKDMIVENDA MNNVFAKLKN NSGKKITVML
DAHTDEVGFM VQAINDNGLL SIVKLGGWHN TTIPAHTVYI KNRDGELIRG ITTSKPSHFM
TAAEKSSNAL EIEDIFIDVG ASSKEEVIDI FKIKVGDPVA PNVEFDFNEK TGVCFGKAFD
NRVGCFCIIQ TLKALADIID LEVDVVGAFA AQEEVGIRGA QITTEVVNPD LAIVFEGSPA
DDLYYSKNIS QGALKKGTQI RNLDQGYIAN PLFIRYAEDI ADKNSIKYQN AVRRGGSTDA
AKISLGNKAV PCLVLGIPSR YVHSHYNYCA KEDIEASVSL AVEVIKNLNE ESINKIMRK
//
