ID A0A3P1S4C6_9FIRM Unreviewed; 411 AA.
AC A0A3P1S4C6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:RRC92098.1};
GN ORFNames=EII25_04650 {ECO:0000313|EMBL:RRC92098.1};
OS Erysipelotrichaceae bacterium OH741_COT-311.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=2491058 {ECO:0000313|EMBL:RRC92098.1, ECO:0000313|Proteomes:UP000270315};
RN [1] {ECO:0000313|EMBL:RRC92098.1, ECO:0000313|Proteomes:UP000270315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH741_COT-311 {ECO:0000313|EMBL:RRC92098.1,
RC ECO:0000313|Proteomes:UP000270315};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RRC92098.1}.
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DR EMBL; RQZE01000007; RRC92098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1S4C6; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000270315; 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:SF3; AMINOPEPTIDASE AMPS; 1.
DR Pfam; PF02073; Peptidase_M29; 1.
DR PRINTS; PR00919; THERMOPTASE.
DR SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:RRC92098.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000270315}.
SQ SEQUENCE 411 AA; 46058 MW; F18CEE5582EB082E CRC64;
MFDQNLLKKY ARLAIRNGVN VAKGQLLVIK AEVSSVDFVR HLVEEAYEYG AKEVVVLWSD
AFIDRLNVKH QDVETLTRIP QWIIDRQQDF VDRGVCFLHV SSEVPGLLKD MDPSKLKQRT
MAVSKAMEPF RYYTMSDVGQ WTIVALPNPT WAKMIFPDLD EEAAMQASFE AMLKAVRVDK
DNDPIAEWDQ HNETLHRHSA LLNNYNFKSL HFKNSLGTDL VVDLAINHIW AGGSSTSQKG
IVFNPNMPTE EVFTMPKRDG VNGVVVATKP LSYQGKLIEN FKIEFKDGKA VKWEAEKGED
ALTNLIHLDD NSSYLGEVAL ISHDSPISNL NLLFYNTLFD ENASCHLALG AAYPSNVKGG
IEMSKEELLK AGANVSMAHS DFMFGSACMS IVGTTFDQQE VVIFKDGNFV I
//
