ID A0A329LMF3_9BACL Unreviewed; 371 AA.
AC A0A329LMF3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:RAV08658.1};
GN ORFNames=DQG23_40775 {ECO:0000313|EMBL:RAV08658.1};
OS Paenibacillus contaminans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=450362 {ECO:0000313|EMBL:RAV08658.1, ECO:0000313|Proteomes:UP000250369};
RN [1] {ECO:0000313|EMBL:RAV08658.1, ECO:0000313|Proteomes:UP000250369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CKOBP-6 {ECO:0000313|EMBL:RAV08658.1,
RC ECO:0000313|Proteomes:UP000250369};
RX PubMed=19126735; DOI=10.1099/ijs.0.001495-0;
RA Chou J.H., Lee J.H., Lin M.C., Chang P.S., Arun A.B., Young C.C.,
RA Chen W.M.;
RT "Paenibacillus contaminans sp. nov., isolated from a contaminated
RT laboratory plate.";
RL Int. J. Syst. Evol. Microbiol. 59:125-129(2009).
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:RAV08658.1}.
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DR EMBL; QMFB01000057; RAV08658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329LMF3; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000250369; 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:RAV08658.1}; 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:UP000250369}.
SQ SEQUENCE 371 AA; 41856 MW; 8FCCE5FCC095B49A CRC64;
MLDPRLTKLA DVLVNYSTRV QQGEHVLIEA TGIEPPLVNE LIKAVQQAGG YPHVKLRDPS
VIRQLLMGAT EEQIRVWMEN DLAEMEKMQA YIAVRGGSNI YEHSDVPSER RKLYSSIYQQ
KVHFDTRVNK TKWVVLRYPS PSMAQLARMS TEAFEQFYFD VCTLDYGKMS KAMDPLKALM
DTTDQVRIVG QGTDLTFSIK GIGAIKCPGG CNIPDGEVYT APVRDSVNGT ITYNAPTPYE
GFTHENVKLE FVNGQIVKAS SNDTDRINRV LDTDEGARYI GEFAIGVNPF IREPMQDILF
DEKIDGSFHF TPGNSYEDAF NGNRSAVHWD MVCIQRPEYG GGEIWFDGKL IRKDGRFVLP
ELEPLNPENL K
//
