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Database: UniProt
Entry: A0A261QJB4_9BACI
LinkDB: A0A261QJB4_9BACI
Original site: A0A261QJB4_9BACI 
ID   A0A261QJB4_9BACI        Unreviewed;       412 AA.
AC   A0A261QJB4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:OZI12898.1};
GN   ORFNames=CEW92_03955 {ECO:0000313|EMBL:OZI12898.1};
OS   Bacillaceae bacterium SAS-127.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX   NCBI_TaxID=2015203 {ECO:0000313|EMBL:OZI12898.1, ECO:0000313|Proteomes:UP000217062};
RN   [1] {ECO:0000313|EMBL:OZI12898.1, ECO:0000313|Proteomes:UP000217062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAS-127 {ECO:0000313|EMBL:OZI12898.1,
RC   ECO:0000313|Proteomes:UP000217062};
RA   Verma A., Pal Y., Krishnamurthi S.;
RT   "Indiibacillus sp. (SAS-127) genome sequencing.";
RL   Submitted (JUN-2017) 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:OZI12898.1}.
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DR   EMBL; NKXN01000018; OZI12898.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261QJB4; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000217062; 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:OZI12898.1}; 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:UP000217062}.
SQ   SEQUENCE   412 AA;  45621 MW;  F9C96DB22FA140C3 CRC64;
     MTNFQQTLEK YAELAVKVGV NIQPGQTLVI NASTDSTEFV RLIVEKAYET GAKHVNVEWS
     DDAVTRLKYD LAPDEAFHEF PKWRAQMLEE LAEEGAAFMS VISSSPDLLK GVQSERIVNA
     QKASGQALNK YRQFIQSDKV SWCVVASPSA AWAQKVFPNL PQEEQVSALW EAIFKAVRAD
     VDQPVEAWKQ HDQALHTKVD YLNSRGYKSL HYTAPGTDLT IDLPEGHLWV GAGSVNEKGH
     EFMANMPTEE VFTVPHKTGV NGHVSSTKPL SYGGNIIDEF TVTFENGRIT EVTAKEGEEV
     LKKLVETDEG SHYLGEIALV PHHSPISESN ILFYNTLFDE NASNHLAIGS AYAFCIEGGK
     TMSQEELEKN GLNTSITHVD FMIGSEQMNI DGITADGQKE PIFRNGNWAE GI
//
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