ID A0A2V2FUN4_9FIRM Unreviewed; 409 AA.
AC A0A2V2FUN4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Aminopeptidase II {ECO:0000313|EMBL:PXX77787.1};
GN ORFNames=DES51_10938 {ECO:0000313|EMBL:PXX77787.1};
OS Dielma fastidiosa.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Dielma.
OX NCBI_TaxID=1034346 {ECO:0000313|EMBL:PXX77787.1, ECO:0000313|Proteomes:UP000247612};
RN [1] {ECO:0000313|EMBL:PXX77787.1, ECO:0000313|Proteomes:UP000247612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC118 {ECO:0000313|EMBL:PXX77787.1,
RC ECO:0000313|Proteomes:UP000247612};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-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:PXX77787.1}.
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DR EMBL; QJKH01000009; PXX77787.1; -; Genomic_DNA.
DR RefSeq; WP_022938983.1; NZ_QJKH01000009.1.
DR AlphaFoldDB; A0A2V2FUN4; -.
DR STRING; 1034346.GCA_000313565_02699; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000247612; 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:PXX77787.1}; 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:UP000247612}.
SQ SEQUENCE 409 AA; 46065 MW; E62449A9F767AA21 CRC64;
MKKCLDKYAE LIIKKGVNLQ PDQPLIVNAP VTSYELVRQL CKKAYEAGAC EVYINWKDDL
IKRYDLEYQS EERLSKPHSW FIDARLEPIK EGAAVASIAS PTPKYLKGVD SQKVNLANEV
LDRALKPFYD ATRSDQNEWC VFADSNPAWA KAVFPELDEK EAEDKLWDAI LKAVYIDEEN
DAMAAWDEHD RLLSERCDKL NQKAFKALHF KNEKGTNLYV GLPEGHIWSG GGEKSQKGVF
FNANMPTEEI FTAPMKWQVN GKVVATKPLD HSGSLIENFW FEFKDGKVID FCAEKEADAL
KRILEADEGS CYLGEVALVE HESPISQSGI LFYNTLFDEN ASCHLALGAA YPLSVEGGCE
MSPEKMAEVG VNDSIKHVDF MFGDETMCIR GLDQDGNETL IFENGRFVL
//
