ID V6M7R5_9BACL Unreviewed; 371 AA.
AC V6M7R5;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:EST54317.1};
GN ORFNames=T458_13360 {ECO:0000313|EMBL:EST54317.1};
OS Brevibacillus panacihumi W25.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1408254 {ECO:0000313|EMBL:EST54317.1, ECO:0000313|Proteomes:UP000017973};
RN [1] {ECO:0000313|EMBL:EST54317.1, ECO:0000313|Proteomes:UP000017973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W25 {ECO:0000313|EMBL:EST54317.1,
RC ECO:0000313|Proteomes:UP000017973};
RX PubMed=24459276;
RA Wang X., Jin D., Zhou L., Wu L., An W., Chen Y., Zhao L.;
RT "Draft Genome Sequence of Brevibacillus panacihumi Strain W25, a
RT Halotolerant Hydrocarbon-Degrading Bacterium.";
RL Genome Announc. 2:e01215-13(2014).
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:EST54317.1}.
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DR EMBL; AYJU01000016; EST54317.1; -; Genomic_DNA.
DR RefSeq; WP_023556591.1; NZ_KI629782.1.
DR AlphaFoldDB; V6M7R5; -.
DR PATRIC; fig|1408254.3.peg.2636; -.
DR eggNOG; COG2309; Bacteria.
DR HOGENOM; CLU_057697_0_0_9; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000017973; 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:SF1; BLL6088 PROTEIN; 1.
DR Pfam; PF02073; Peptidase_M29; 1.
DR SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:EST54317.1}; 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:UP000017973}.
SQ SEQUENCE 371 AA; 42321 MW; 57DB3FAAE49C0D52 CRC64;
MADPRINELA SRLIRYSLNL QKGEKLLIEN TGLQPELVRA LVREAFAVGA LPLVTLKDQE
VLRALYEGTS EEHMALMAKY EYERMKDMDA YIAIRAYENI NELSDVPEDK MGIYARVLYQ
KVHTNERIAN KRWVVLRYPN KSMAQLSNMS LERFENFYFD VCNLDYAKMS RAMTPLKELM
DRTDRVRIVG PKTDLRFSIK GIGAIKCDGK RNIPDGEVYT APVRDSVEGT IYYNAATNYN
GTTFTDVQFT FKEGKIVEAT SSNTKALNDI LDTDEGSRYI GEFAIGFNPH ILHPMLDILF
DEKIAGSFHF TPGNAYNVAD NGNRSSVHWD LVQIQRPEYG GGEIWFDDVL IRKDGRFVLP
ELEGLNPENL V
//
