ID A0A372LJC2_9BACI Unreviewed; 410 AA.
AC A0A372LJC2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:RFU66185.1};
GN ORFNames=D0469_17775 {ECO:0000313|EMBL:RFU66185.1};
OS Peribacillus saganii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=2303992 {ECO:0000313|EMBL:RFU66185.1, ECO:0000313|Proteomes:UP000264541};
RN [1] {ECO:0000313|EMBL:RFU66185.1, ECO:0000313|Proteomes:UP000264541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V47-23a {ECO:0000313|EMBL:RFU66185.1,
RC ECO:0000313|Proteomes:UP000264541};
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:RFU66185.1}.
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DR EMBL; QVTE01000052; RFU66185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372LJC2; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000264541; 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:RFU66185.1}; 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:UP000264541}.
SQ SEQUENCE 410 AA; 45595 MW; 53E3C1BDBE89354D CRC64;
MKDFQKQLEK YAELAVKVGV NIQKGQTLVV NVLLEGAELA RLIAKKAYEA GASNVIVNFS
DDTLSRLKYD MASDEVFTEY PEHRAKEQIE LAEKGAAFLH ILSSSPALLK GVKPERISSF
QKAAGAALKQ YRQMVQSDKV SWSIIAVPSQ AWADMVFPEE PAESRVDLLW EAIFKTVRID
KEKPVEAWKT HNETLHKKVD YLNGKHYKKL HYRAPGTDLT IELPEKHIWV GAGSVNEKGI
DFMANMPTEE VFTVPLKTGV NGTVSSTKPL SYGGNIIDNF MITFKDGRIV DVKAEEGEEI
LKQLVETDEG SHYLGEVALV PFNSPISQSN ILFYNTLFDE NASNHLAIGS SYSFCLEGGK
KMSPEELAEH GLNESLTHVD FMIGSAEMDI DGIKENGTSE PVFKNGDWAF
//
