ID A0A099RPM0_9CLOT Unreviewed; 345 AA.
AC A0A099RPM0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:KGK81731.1};
GN ORFNames=DP68_18050 {ECO:0000313|EMBL:KGK81731.1};
OS Clostridium sp. HMP27.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1487921 {ECO:0000313|EMBL:KGK81731.1, ECO:0000313|Proteomes:UP000030009};
RN [1] {ECO:0000313|EMBL:KGK81731.1, ECO:0000313|Proteomes:UP000030009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMP27 {ECO:0000313|EMBL:KGK81731.1,
RC ECO:0000313|Proteomes:UP000030009};
RA Tan B.F., Foght J., Budwill K.;
RT "Draft genome sequence of Clostridium sp. HMP27 isolated from a coal
RT degrading methanogenic culture.";
RL Submitted (APR-2014) 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}.
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:KGK81731.1}.
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DR EMBL; JMFY01000058; KGK81731.1; -; Genomic_DNA.
DR RefSeq; WP_035311842.1; NZ_JMFY01000058.1.
DR AlphaFoldDB; A0A099RPM0; -.
DR STRING; 1487921.DP68_18050; -.
DR MEROPS; M42.A02; -.
DR eggNOG; COG1363; Bacteria.
DR Proteomes; UP000030009; 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:KGK81731.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030009}.
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 345 AA; 38030 MW; 238A21C0C96EA76D CRC64;
MNYNEEQIKY YLSNILTTPS PSGYTKKVIA YIKKELDIIG VSYELTNKGC ILVTLPGKDK
QNGRVLSAHI DTLGAMVKGI KSNGTLSLAA IGGYMMNSIE GENCIIETLD GKEFTGTIQS
IKPSVHISGD EARELKRTVE NMEIVLDEKV FCREDTLELG IEVGDFVSFD SRTVFTPSGF
VKSRHLDDKA SAAILLYAIK YLVDNKIDLP YTTSFFITNY EEVGHGAAAI PHNTKEFIAV
DMGAPGLDQN SSEYAVCICA KDSSGPYDLE TRKKLIDLCR KNDIPYKIDI YPYYGSDASS
ALRAGWDIKT GLIGTGVFAS HGYERTHMDG ILATLDLVIN YCKED
//
