ID A0A2B6C3E8_BACAN Unreviewed; 332 AA. AC A0A2B6C3E8; A0A1Q4M6S3; E9QX86; E9QX87; Q6HTS7; Q6KN14; Q81MC5; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 27-MAR-2024, entry version 17. DE RecName: Full=Proline iminopeptidase {ECO:0000256|ARBA:ARBA00021843}; DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568}; DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00029605}; GN OrderedLocusNames=GBAA_4324 {ECO:0000313|EMBL:AAT33446.1}; OS Bacillus anthracis. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392 {ECO:0000313|EMBL:AAT33446.1, ECO:0000313|Proteomes:UP000000594}; RN [1] {ECO:0000313|EMBL:AAT33446.1, ECO:0000313|Proteomes:UP000000594} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames ancestor {ECO:0000313|Proteomes:UP000000594}; RX PubMed=18952800; DOI=10.1128/JB.01347-08; RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.; RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."; RL J. Bacteriol. 191:445-446(2009). CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; CC Evidence={ECO:0000256|ARBA:ARBA00001585}; CC -!- SIMILARITY: Belongs to the peptidase S33 family. CC {ECO:0000256|ARBA:ARBA00010088}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017334; AAT33446.1; -; Genomic_DNA. DR RefSeq; WP_000898981.1; NZ_WXXJ01000027.1. DR AlphaFoldDB; A0A2B6C3E8; -. DR IntAct; A0A2B6C3E8; 2. DR GeneID; 45023992; -. DR KEGG; bar:GBAA_4324; -. DR PATRIC; fig|1392.230.peg.4269; -. DR OMA; WFENSAH; -. DR OrthoDB; 53505at2; -. DR Proteomes; UP000000594; Chromosome. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR002410; Peptidase_S33. DR PANTHER; PTHR43329:SF1; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR43329; EPOXIDE HYDROLASE; 1. DR Pfam; PF00561; Abhydrolase_1; 1. DR PRINTS; PR00793; PROAMNOPTASE. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000313|EMBL:AAT33446.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000594}. FT DOMAIN 47..158 FT /note="AB hydrolase-1" FT /evidence="ECO:0000259|Pfam:PF00561" SQ SEQUENCE 332 AA; 38270 MW; CF149E930B4F808B CRC64; MLFRSYTPQF YNENKQPIPN SIATMESVMI NNRKQTLLIR GQNVEQPILL CCHGGPGMAQ IGFIRHFQKE LEKHFIVINW DQRGAGKSFS TKDFGANFTI EQFISDAKEV IQYVLKKFSK QKLFLAGHSW GSIIGLNIAH QYPQYIEAYI GIGQIVHMKQ NEELLYQHLI RSAKKHDHKK ALASLLKLGK PPFLDTRRLI IQRKWLGTFG GAIQNGSSFS FIRKGFFSPE YTLLDWFKFL AGNLKSGVLW EEMLTIDFFS SITSLSIPVY FCSGRYDYQT PYALVQEYCD VIEAPIKKMI WFPNSAHSPD LEEPELFAHS LQSIKQELAF QH //