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Database: UniProt
Entry: A0A1H6WZJ2_9FIRM
LinkDB: A0A1H6WZJ2_9FIRM
Original site: A0A1H6WZJ2_9FIRM 
ID   A0A1H6WZJ2_9FIRM        Unreviewed;       410 AA.
AC   A0A1H6WZJ2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Leucyl aminopeptidase (Aminopeptidase T) {ECO:0000313|EMBL:SEJ22313.1};
GN   ORFNames=SAMN05660742_104219 {ECO:0000313|EMBL:SEJ22313.1};
OS   Propionispira arboris.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Propionispira.
OX   NCBI_TaxID=84035 {ECO:0000313|EMBL:SEJ22313.1, ECO:0000313|Proteomes:UP000199662};
RN   [1] {ECO:0000313|EMBL:SEJ22313.1, ECO:0000313|Proteomes:UP000199662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2179 {ECO:0000313|EMBL:SEJ22313.1,
RC   ECO:0000313|Proteomes:UP000199662};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNZK01000004; SEJ22313.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6WZJ2; -.
DR   STRING; 84035.SAMN05660742_104219; -.
DR   Proteomes; UP000199662; 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:SEJ22313.1}; 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:UP000199662}.
SQ   SEQUENCE   410 AA;  45808 MW;  9019C5F803F13C64 CRC64;
     MQNKLEKYAR LVIHTGVNLK KDQLLVINSP IECAPFTRLL ATTAYNAGAK EVIVSWNDEK
     LEKIRFTMAP EEVFDAFPEW RKQLYIGYAK QEAAFISIAA SDPEIFKAVN VDRMARAQKS
     SSTALKEYRE RMMSNQNAWC VVSIPTAAWA GKVFPEMQTA EAVDKLWQTI FQTVRIDAES
     DPVKNWEKHL GNLEKAKDFM NQYAFKYLHY KNAAGTDLKI ELPDGHLWIS GAELTPDKRP
     FVANMPTEEV YSMPKADGVN GTVVSSKPLN YHGNLIDKFT LTFEAGKVIA YSAEQGQEIL
     AKLLETDEGS ARLGEVALVP YDSPISNSKI LFYNTLFDEN ASCHLAFGKA YPVCIKNGEN
     MSAKELHKAG VNDSLVHEDF MVGTEDLEIT GIMKDGTAVA VFKNGNFVSF
//
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