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
//