ID   APEB_STRCO              Reviewed;         432 AA.
AC   Q9XA76;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Probable M18 family aminopeptidase 2;
DE            EC=3.4.11.-;
GN   Name=apeB; OrderedLocusNames=SCO3801; ORFNames=SCGD3.02;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
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DR   EMBL; AL939117; CAB46924.1; -; Genomic_DNA.
DR   PIR; T36482; T36482.
DR   RefSeq; NP_627990.1; NC_003888.3.
DR   RefSeq; WP_003975140.1; NZ_VNID01000003.1.
DR   AlphaFoldDB; Q9XA76; -.
DR   SMR; Q9XA76; -.
DR   STRING; 100226.SCO3801; -.
DR   GeneID; 1099237; -.
DR   KEGG; sco:SCO3801; -.
DR   PATRIC; fig|100226.15.peg.3869; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_2_0_11; -.
DR   InParanoid; Q9XA76; -.
DR   OMA; GPILKVN; -.
DR   PhylomeDB; Q9XA76; -.
DR   Proteomes; UP000001973; 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_0000173469"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         408
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   432 AA;  45971 MW;  DE8AE18F372F1F20 CRC64;
     MSAPSRFDRG HTDDLMTFLS ASPTPYHAVA SAAARLEKAG FRQVAETDAW EATSGGKYVL
     RGGAIVAWYV PEGAAAHTPF RIVGAHTDSP NLRVKPRPDT GAHGWRQVAV EIYGGPLMNS
     WLDRDLGLAG RLSLRDGSTR LVDVDRPLLR VPQLAIHMDR NVSTEGLKLD KQRHLQPVWG
     LGDSVRDGDL IAFLEDEAGL ARGEVTGWDL MTHSVEPPAY LGRDRELVAG PRMDNLLSVH
     AGTAALASVA ASGADLPYIP VLAAFDHEET GSQSDTGADG PLLGGVLERS VFARGGSYED
     RARAFAGTVC LSSDTGHAVH PNYAERHDPT HHPRINGGPI LKVNVNNRYA TDGSGRAVFA
     AACEKADIPF QTFVSNNSMP CGTTIGPITA ARHGISTVDI GVAILSMHSA RELCGADDPH
     LLANALVAFL QP