ID PAC_LYSSH Reviewed; 338 AA. AC P12256; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 24-JAN-2024, entry version 98. DE RecName: Full=Penicillin acylase; DE EC=3.5.1.11; DE AltName: Full=Penicillin V amidase; DE Short=PVA; DE Flags: Precursor; OS Lysinibacillus sphaericus (Bacillus sphaericus). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus. OX NCBI_TaxID=1421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3026906; DOI=10.1016/0378-1119(86)90252-0; RA Olsson A., Uhlen M.; RT "Sequencing and heterologous expression of the gene encoding penicillin V RT amidase from Bacillus sphaericus."; RL Gene 45:175-181(1986). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 4-338, AND PROTEIN SEQUENCE OF RP N-TERMINUS. RX PubMed=10331865; DOI=10.1038/8213; RA Suresh C.G., Pundle A.V., SivaRaman H., Rao K.N., Brannigan J.A., RA McVey C.E., Verma C.S., Dauter Z., Dodson E.J., Dodson G.G.; RT "Penicillin V acylase crystal structure reveals new Ntn-hydrolase family RT members."; RL Nat. Struct. Biol. 6:414-416(1999). CC -!- FUNCTION: The enzyme catalyzes the conversion of penicillin to 6- CC aminopenicillanate The precursor, furthermore, acts as a self- CC processing peptidase that cleaves off the propeptide. All peptidase CC activity is lost on conversion to the mature peptidase. CC -!- CATALYTIC ACTIVITY: CC Reaction=a penicillin + H2O = 6-aminopenicillanate + a carboxylate; CC Xref=Rhea:RHEA:18693, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, CC ChEBI:CHEBI:51356, ChEBI:CHEBI:57869; EC=3.5.1.11; CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the peptidase C59 family. {ECO:0000305}. 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; M15660; AAA22654.1; -; Genomic_DNA. DR PIR; A25559; A25559. DR PDB; 2IWM; X-ray; 2.50 A; A/B/C/D=1-338. DR PDB; 2PVA; X-ray; 2.50 A; A/B/C/D=4-338. DR PDB; 2QUY; X-ray; 1.70 A; A/B/C/D/E/F/G/H=4-338. DR PDB; 2Z71; X-ray; 2.60 A; A/C=4-338. DR PDB; 3MJI; X-ray; 2.50 A; A/B/C/D=1-338. DR PDB; 3PVA; X-ray; 2.80 A; A/B/C/D/E/F/G/H=4-338. DR PDBsum; 2IWM; -. DR PDBsum; 2PVA; -. DR PDBsum; 2QUY; -. DR PDBsum; 2Z71; -. DR PDBsum; 3MJI; -. DR PDBsum; 3PVA; -. DR AlphaFoldDB; P12256; -. DR SMR; P12256; -. DR STRING; 1421.A2J09_09020; -. DR DrugBank; DB01822; (4R,5R)-1,2-dithiane-4,5-diol. DR DrugBank; DB03661; L-cysteic acid. DR DrugBank; DB00417; Phenoxymethylpenicillin. DR MEROPS; C59.001; -. DR BRENDA; 3.5.1.11; 698. DR EvolutionaryTrace; P12256; -. DR GO; GO:0008953; F:penicillin amidase activity; IEA:UniProtKB-EC. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR CDD; cd00542; Ntn_PVA; 1. DR InterPro; IPR029132; CBAH/NAAA_C. DR InterPro; IPR029055; Ntn_hydrolases_N. DR PANTHER; PTHR35527; CHOLOYLGLYCINE HYDROLASE; 1. DR PANTHER; PTHR35527:SF2; HYDROLASE-RELATED; 1. DR Pfam; PF02275; CBAH; 1. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic resistance; Direct protein sequencing; Hydrolase; KW Zymogen. FT PROPEP 1..3 FT /note="Removed in mature form" FT /evidence="ECO:0000269|PubMed:10331865" FT /id="PRO_0000045278" FT CHAIN 4..338 FT /note="Penicillin acylase" FT /id="PRO_0000045279" FT ACT_SITE 4 FT STRAND 5..10 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 16..26 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 31..35 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:2IWM" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:2Z71" FT STRAND 57..62 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 69..75 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 80..85 FT /evidence="ECO:0007829|PDB:2QUY" FT TURN 87..89 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:2QUY" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:2QUY" FT HELIX 108..115 FT /evidence="ECO:0007829|PDB:2QUY" FT HELIX 119..127 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 129..132 FT /evidence="ECO:0007829|PDB:2QUY" FT TURN 137..139 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 145..150 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 156..162 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 165..169 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:2QUY" FT HELIX 182..188 FT /evidence="ECO:0007829|PDB:2QUY" FT HELIX 189..192 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 208..210 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 213..215 FT /evidence="ECO:0007829|PDB:2QUY" FT HELIX 217..219 FT /evidence="ECO:0007829|PDB:2QUY" FT HELIX 228..241 FT /evidence="ECO:0007829|PDB:2QUY" FT HELIX 248..260 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 268..270 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 278..286 FT /evidence="ECO:0007829|PDB:2QUY" FT TURN 287..290 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 291..296 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 299..307 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 318..321 FT /evidence="ECO:0007829|PDB:2QUY" FT STRAND 329..331 FT /evidence="ECO:0007829|PDB:2QUY" SQ SEQUENCE 338 AA; 37458 MW; 69C8A9F69BB084B3 CRC64; MLGCSSLSIR TTDDKSLFAR TMDFTMEPDS KVIIVPRNYG IRLLEKENVV INNSYAFVGM GSTDITSPVL YDGVNEKGLM GAMLYYATFA TYADEPKKGT TGINPVYVIS QVLGNCVTVD DVIEKLTSYT LLNEANIILG FAPPLHYTFT DASGESIVIE PDKTGITIHR KTIGVMTNSP GYEWHQTNLR AYIGVTPNPP QDIMMGDLDL TPFGQGAGGL GLPGDFTPSA RFLRVAYWKK YTEKAKNETE GVTNLFHILS SVNIPKGVVL TNEGKTDYTI YTSAMCAQSK NYYFKLYDNS RISAVSLMAE NLNSQDLITF EWDRKQDIKQ LNQVNVMS //