ID A0A1D8AY03_9BACT Unreviewed; 372 AA.
AC A0A1D8AY03;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Aminopeptidase T {ECO:0000313|EMBL:AOS45779.1};
DE EC=3.4.11.- {ECO:0000313|EMBL:AOS45779.1};
GN ORFNames=Verru16b_02867 {ECO:0000313|EMBL:AOS45779.1};
OS Lacunisphaera limnophila.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Lacunisphaera.
OX NCBI_TaxID=1838286 {ECO:0000313|EMBL:AOS45779.1, ECO:0000313|Proteomes:UP000095228};
RN [1] {ECO:0000313|EMBL:AOS45779.1, ECO:0000313|Proteomes:UP000095228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IG16b {ECO:0000313|EMBL:AOS45779.1,
RC ECO:0000313|Proteomes:UP000095228};
RA Rast P., Gloeckner I., Jogler M., Boedeker C., Jeske O., Wiegand S.,
RA Reinhardt R., Schumann P., Rohde M., Spring S., Gloeckner F.O., Jogler C.;
RT "Three novel species with peptidoglycan cell walls form the new genus
RT Lacunisphaera gen. nov. in the family Opitutaceae of the verrucomicrobial
RT subdivision 4.";
RL Submitted (JUN-2016) 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}.
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DR EMBL; CP016094; AOS45779.1; -; Genomic_DNA.
DR RefSeq; WP_069962892.1; NZ_CP016094.1.
DR AlphaFoldDB; A0A1D8AY03; -.
DR STRING; 1838286.Verru16b_02867; -.
DR KEGG; obg:Verru16b_02867; -.
DR PATRIC; fig|1838286.3.peg.2881; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000095228; Chromosome.
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:AOS45779.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AOS45779.1};
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:UP000095228}.
SQ SEQUENCE 372 AA; 41448 MW; FCAB881F02FD466D CRC64;
MSDSRYNQLA EVLTGFSCDL KKGERVLIDA FDVPEGFVIA LVRATRALGA IPYVNLQNAR
ITRELLQGAS TDQYRLTADI ELARMQKMDA YIAARGSHNI FETSDVPAAR VQLVAKLMKP
VLDYRVNKTK WVVLRWPSSA MAQQAGMSTE AFEDFYFKVC TFDYRRYGPG MAALEDLMNR
TDRVHLKGPG TDLKFSIKGI GAEACGGLRN IPDGEVFSCP VKDSVEGVIQ YNAPTVYLGT
AFDNIRLVFK QGKIVEATAN NTKRLNEILD TDAGARYIGE FAIGFNPHIT EPMRDILFDE
KIAGSFHFTP GKAYERAGNG NESVVHWDMV NIQRPEYGGG EIWFDGKLIR KDGLFVLPAL
KKLNPDQLLK KG
//
