PAC_LYSSH
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 25-MAY-2022, entry version 94.
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; Firmicutes; 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=H2O + penicillin = 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}.
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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 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 InterPro; IPR029132; CBAH/NAAA_C.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR Pfam; PF02275; CBAH; 1.
DR SUPFAM; SSF56235; SSF56235; 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
