ID G2FQJ2_9FIRM Unreviewed; 372 AA.
AC G2FQJ2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:EGW40057.1};
DE EC=3.4.11.- {ECO:0000313|EMBL:EGW40057.1};
GN Name=ampS {ECO:0000313|EMBL:EGW40057.1};
GN ORFNames=DOT_1772 {ECO:0000313|EMBL:EGW40057.1};
OS Desulfosporosinus sp. OT.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW40057.1, ECO:0000313|Proteomes:UP000004928};
RN [1] {ECO:0000313|EMBL:EGW40057.1, ECO:0000313|Proteomes:UP000004928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT {ECO:0000313|EMBL:EGW40057.1,
RC ECO:0000313|Proteomes:UP000004928};
RX PubMed=21994931; DOI=10.1128/JB.06018-11;
RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL J. Bacteriol. 193:6104-6105(2011).
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M29 family.
CC {ECO:0000256|ARBA:ARBA00008236}.
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:EGW40057.1}.
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DR EMBL; AGAF01000095; EGW40057.1; -; Genomic_DNA.
DR RefSeq; WP_009617026.1; NZ_AGAF01000095.1.
DR AlphaFoldDB; G2FQJ2; -.
DR PATRIC; fig|913865.3.peg.1809; -.
DR eggNOG; COG2309; Bacteria.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000004928; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR InterPro; IPR035097; M29_N-terminal.
DR InterPro; IPR000787; Peptidase_M29.
DR PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR34448:SF1; BLL6088 PROTEIN; 1.
DR Pfam; PF02073; Peptidase_M29; 1.
DR SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:EGW40057.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGW40057.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
SQ SEQUENCE 372 AA; 41839 MW; 59BF58D06458DD71 CRC64;
MKDPRIEKLA NSLINYSIAL QPGEKILIEV IGQDIPLAQA LVRYAYQAGG LPFLSTINNT
LQRELLKEFT VEQAEAMTRW DLARMREMQA FIGIRAGENA NEWADVPSDA MRTYASHYLK
PVHTEQRVAH TRWCVLRYPN ASMAQLGNMS IEGFEDFYFD VCNLDYSKMS RAMEPLKALM
EKTDQVHIIG PGTDLIFSII GMPAIKCDGH VNIPDGEIFS APVKESVNGQ ISYNTPSLYQ
GFTYENIVLE FKDGKIVKAT SNDSDRIETV FNTDDGARYV GEFAIGVNPF IQTPMKDTLF
DEKIDGSFHF TPGASYDDCS NGNKSAIHWD LVCIQRPEYG GGEIYFDKTL VRKDGRFVLP
ELEALNPENL KS
//
