APEB_STRAW
ID APEB_STRAW Reviewed; 432 AA.
AC Q82F74;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_00467};
DE EC=3.4.11.- {ECO:0000255|HAMAP-Rule:MF_00467};
GN Name=apeB {ECO:0000255|HAMAP-Rule:MF_00467}; OrderedLocusNames=SAV_4389;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00467};
CC -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000255|HAMAP-
CC Rule:MF_00467}.
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DR EMBL; BA000030; BAC72101.1; -; Genomic_DNA.
DR RefSeq; WP_010985814.1; NZ_JZJK01000079.1.
DR AlphaFoldDB; Q82F74; -.
DR SMR; Q82F74; -.
DR STRING; 227882.SAV_4389; -.
DR EnsemblBacteria; BAC72101; BAC72101; SAVERM_4389.
DR KEGG; sma:SAVERM_4389; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_019532_2_0_11; -.
DR OMA; GPILKVN; -.
DR OrthoDB; 304020at2; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.250.10; -; 1.
DR HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR InterPro; IPR022984; M18_aminopeptidase_2.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; PTHR28570; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..432
FT /note="Probable M18 family aminopeptidase 2"
FT /id="PRO_0000173468"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00467"
SQ SEQUENCE 432 AA; 46013 MW; 5700C669FFF4AEC3 CRC64;
MSNPVRFDRG HTDDLMSFLA ASPSPYHAVT NAAERLEKAG FRQVAETDAW DSTSGGKYVV
RGGALIAWYV PEGADPHTPF RIVGAHTDSP NLRVKPRPDS GAHGWRQIAV EIYGGPLLNS
WLDRDLGLAG RLSLRDGSTR LVNIDRPLLR VPQLAIHLDR SVSTDGLKLD KQRHLQPIWG
LGGDVRDGDL IAFLEAELGL SAGEVTGWDL MTHSVEAPSY LGRDNELLAG PRMDNLLSVH
AGTAALTAVA AADASLAYIP VLAAFDHEEN GSQSDTGADG PLLGSVLERS VFARSGSYED
RARAFAGSVC LSSDTGHAVH PNYAERHDPT HHPRAGGGPI LKVNVNNRYA TDGSGRAIFA
AACEKANVPF QTFVSNNSMP CGTTIGPITA ARHGIRTVDI GAAILSMHSA RELCATDDPF
LLANSLVAFL EG