ID A0A1L8QRY3_9ENTE Unreviewed; 411 AA.
AC A0A1L8QRY3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Aminopeptidase PepS {ECO:0000313|EMBL:OJG10239.1};
GN ORFNames=RU93_GL002264 {ECO:0000313|EMBL:OJG10239.1};
OS Enterococcus aquimarinus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=328396 {ECO:0000313|EMBL:OJG10239.1, ECO:0000313|Proteomes:UP000182149};
RN [1] {ECO:0000313|EMBL:OJG10239.1, ECO:0000313|Proteomes:UP000182149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17690 {ECO:0000313|EMBL:OJG10239.1,
RC ECO:0000313|Proteomes:UP000182149};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-2014) 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:OJG10239.1}.
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DR EMBL; JXKD01000009; OJG10239.1; -; Genomic_DNA.
DR RefSeq; WP_071874961.1; NZ_JXKD01000009.1.
DR AlphaFoldDB; A0A1L8QRY3; -.
DR STRING; 328396.RU93_GL002264; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000182149; 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:OJG10239.1}; 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:UP000182149}.
SQ SEQUENCE 411 AA; 45013 MW; C10299DABF927498 CRC64;
MVLKNFNENL EKYAELIVAI GVNVQKSHTV ILQIDVQQIE LARLITKKAY ELGAAEVIVK
WNDSFIQKEF LLHAEQERLE NIPQYRIDES DDWIEKGASR ISVVSSDPGA LAGVDSTRIA
AYQKAAGKAL ANLRKATQAN KVSWTVVAAA GQEWANKVFP DLAPEAALDA LWEQIFKTTR
IYTEDPVAAW KEHTDTLQGK AEELNKEQFV ALHYTAPGTD LMVGLPKNHV WEGVGSLNAR
GEKFNANMPT EEVFSAPDAN RVDGYVSSSK PLSYAGSIIS GMKFTFKDGK VVDFSAEEGQ
EVLATLLDTD EGARRLGEVA LVPDPSPISQ SGITFFNTLF DENASNHLAF GSAYAFNLQG
GTEMTEEELA AAGLNRSHTH VDFMIGSAEM DIDGIRADGT KVPVFRNGDW A
//
