ID A0A3E2J521_9BACI Unreviewed; 410 AA.
AC A0A3E2J521;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:RFU61073.1};
GN ORFNames=D0463_15595 {ECO:0000313|EMBL:RFU61073.1};
OS Bacillus sp. V59.32b.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1758642 {ECO:0000313|EMBL:RFU61073.1, ECO:0000313|Proteomes:UP000258625};
RN [1] {ECO:0000313|EMBL:RFU61073.1, ECO:0000313|Proteomes:UP000258625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V59.32a {ECO:0000313|EMBL:RFU61073.1,
RC ECO:0000313|Proteomes:UP000258625};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus chawlae sp. nov., Bacillus glennii sp. nov., and Bacillus saganii
RT sp. nov. Isolated from the Vehicle Assembly Building at Kennedy Space
RT Center where the Viking Spacecraft were Assembled.";
RL Submitted (AUG-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:RFU61073.1}.
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DR EMBL; QVTC01000072; RFU61073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2J521; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000258625; 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:RFU61073.1}; 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:UP000258625}.
SQ SEQUENCE 410 AA; 45574 MW; 9326B3E973FC50AE CRC64;
MSNFQGNLEK YAELAVKVGV NVQKGQTLVI NTALEGAALV RLIVKKAYEI GARNVIVNWT
DDTVNRIKYD LAPDEVFTEY PEHRAKEMIE WAEKGAAYLS VISSPPDLLK GVRPERIANF
QKASGTALKQ FRQYMQADKF SWSIVAVPSQ AWADMVFPDA AAEERVHKLW DAIFKATRID
TENPVASWKK HDESLHEKVD YLNGKRYKKL HYKASGTDLT IELPEQHLWV GAGSINEQGH
AFMANMPTEE VFTVPLKTGV NGTVSSTKPL SYGGNIIDKF SITFKEGRIV EVKAEEGEAI
LKQLVETDEG SHYLGEVALV PFNSPISQSN VLFFNTLFDE NASNHLAIGS AYAFCLEGGK
KMSPEELAKN GLNESITHVD FMIGSSQMDI DGIKEDGSTE AIFRKGDWAF
//
