AMPP1_STRCO
ID AMPP1_STRCO Reviewed; 491 AA.
AC P0A3Z1; Q05813;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Xaa-Pro aminopeptidase 1;
DE EC=3.4.11.9;
DE AltName: Full=Aminoacylproline aminopeptidase I;
DE AltName: Full=Aminopeptidase P I;
DE Short=APP;
DE Short=PEPP I;
DE AltName: Full=X-Pro aminopeptidase I;
DE AltName: Full=Xaa-Pro aminopeptidase I;
GN Name=pepPI; Synonyms=pepP; OrderedLocusNames=SCO3970;
GN ORFNames=SCBAC25E3.07c;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Release of any N-terminal amino acid, including proline, that
CC is linked to proline, even from a dipeptide or tripeptide.;
CC EC=3.4.11.9;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; AL939118; CAC44694.1; -; Genomic_DNA.
DR RefSeq; NP_628153.1; NC_003888.3.
DR RefSeq; WP_003974973.1; NZ_VNID01000003.1.
DR AlphaFoldDB; P0A3Z1; -.
DR SMR; P0A3Z1; -.
DR STRING; 100226.SCO3970; -.
DR MEROPS; M24.033; -.
DR GeneID; 1099406; -.
DR KEGG; sco:SCO3970; -.
DR PATRIC; fig|100226.15.peg.4043; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_1_0_11; -.
DR InParanoid; P0A3Z1; -.
DR OMA; GWADTEL; -.
DR PhylomeDB; P0A3Z1; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW Protease; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..491
FT /note="Xaa-Pro aminopeptidase 1"
FT /id="PRO_0000185079"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 308
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 491 AA; 54048 MW; 1FE2C5E8C26C70DF CRC64;
MAEELTPENP AIPETPEETE EPIKQRKNGL YPGVSDELAE NMQSGWADTE LHDLEPIAQA
AETAARRAAL SARFPGERLV IPAGNLKTRS NDTEYSFRAS VEYAYLTGNQ TEDGVLVMEP
EGDGHAATIY LLPRSDRENG EFWLDGQGEL WVGRRHSLAE AGELYGIPAS DVRELAGSLR
EATGPVRVVR GFDAGIEAAL TDKVTAERDE ELRVFLSEAR LVKDEFEIGE LQKAVDSTVR
GFEDVVKVLD RAEATSERYI EGTFFLRARV EGNDVGYGSI CAAGPHACTL HWVRNDGPVR
SGDLLLLDAG VETHTYYTAD VTRTLPISGT YSELQKKIYD AVYDAQEAGI AAVRPGAKYR
DFHDASQRVL AERLVEWGLV EGPVERVLEL GLQRRWTLHG TGHMLGMDVH DCAAARVESY
VDGTLEPGMV LTVEPGLYFQ ADDLTVPEEY RGIGVRIEDD ILVTADGNRN LSAGLPRRSD
EVEEWMAALK G
