ID   PAC_KLUCR               Reviewed;         844 AA.
AC   P07941;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Penicillin G acylase;
DE            EC=3.5.1.11;
DE   AltName: Full=Penicillin G amidase;
DE   AltName: Full=Penicillin amidohydrolase;
DE   Contains:
DE     RecName: Full=Penicillin G acylase subunit alpha;
DE   Contains:
DE     RecName: Full=Penicillin G acylase subunit beta;
DE   Flags: Precursor;
GN   Name=pac;
OS   Kluyvera cryocrescens (Kluyvera citrophila).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Kluyvera.
OX   NCBI_TaxID=580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 21285 / DSM 2660;
RX   PubMed=3032748; DOI=10.1016/0378-1119(86)90386-0;
RA   Barbero J.L., Buesa J.M., de Buitrago G.G., Mendez E., Perez-Aranda A.,
RA   Garcia J.L.;
RT   "Complete nucleotide sequence of the penicillin acylase gene from Kluyvera
RT   citrophila.";
RL   Gene 49:69-80(1986).
RN   [2]
RP   PROTEIN SEQUENCE OF 290-297, AND ACTIVE SITE.
RX   PubMed=1764029; DOI=10.1042/bj2800659;
RA   Martin J., Slade A., Aitken A., Arche R., Virden R.;
RT   "Chemical modification of serine at the active site of penicillin acylase
RT   from Kluyvera citrophila.";
RL   Biochem. J. 280:659-662(1991).
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit processed
CC       from the same precursor.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the peptidase S45 family. {ECO:0000305}.
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DR   EMBL; M15418; AAA25047.1; -; Genomic_DNA.
DR   PIR; A26528; A26528.
DR   PDB; 4PEL; X-ray; 2.80 A; A/C/E/G=1-221, B/D/F/H=290-844.
DR   PDBsum; 4PEL; -.
DR   AlphaFoldDB; P07941; -.
DR   SMR; P07941; -.
DR   STRING; 580.GCA_001266615_00785; -.
DR   MEROPS; S45.001; -.
DR   PRIDE; P07941; -.
DR   BRENDA; 3.5.1.11; 2821.
DR   SABIO-RK; P07941; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008953; F:penicillin amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd03748; Ntn_PGA; 1.
DR   Gene3D; 1.10.1400.10; -; 1.
DR   Gene3D; 1.10.439.10; -; 1.
DR   Gene3D; 2.30.120.10; -; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR014395; Pen/GL7ACA/AHL_acylase.
DR   InterPro; IPR043147; Penicillin_amidase_A-knob.
DR   InterPro; IPR023343; Penicillin_amidase_dom1.
DR   InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR   InterPro; IPR033813; PGA_C.
DR   InterPro; IPR002692; S45.
DR   PANTHER; PTHR34218; PTHR34218; 1.
DR   Pfam; PF01804; Penicil_amidase; 1.
DR   PIRSF; PIRSF001227; Pen_acylase; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic resistance; Calcium; Direct protein sequencing;
KW   Hydrolase; Metal-binding; Periplasm; Signal; Zymogen.
FT   SIGNAL          1..26
FT   CHAIN           27..844
FT                   /note="Penicillin G acylase"
FT                   /id="PRO_0000027349"
FT   CHAIN           27..235
FT                   /note="Penicillin G acylase subunit alpha"
FT                   /id="PRO_0000027350"
FT   PROPEP          236..289
FT                   /note="Spacer peptide"
FT                   /evidence="ECO:0000269|PubMed:1764029"
FT                   /id="PRO_0000027351"
FT   CHAIN           290..844
FT                   /note="Penicillin G acylase subunit beta"
FT                   /id="PRO_0000027352"
FT   ACT_SITE        290
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:1764029"
FT   BINDING         178
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         362
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         364
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         365
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         494
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         540
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   STRAND          32..38
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   STRAND          43..46
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   HELIX           50..64
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   HELIX           68..77
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   HELIX           81..84
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   HELIX           89..97
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   HELIX           101..109
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   HELIX           113..133
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   HELIX           137..140
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   HELIX           143..147
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   HELIX           157..166
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   TURN            167..173
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   HELIX           178..190
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   HELIX           194..204
FT                   /evidence="ECO:0007829|PDB:4PEL"
FT   TURN            218..220
FT                   /evidence="ECO:0007829|PDB:4PEL"
SQ   SEQUENCE   844 AA;  93572 MW;  3466059B0FC4E5AF CRC64;
     MKNRNRMIVN GIVTSLICCS SLSALAASPP TEVKIVRDEY GMPHIYADDT YRLFYGYGYV
     VAQDRLFQME MARRSTQGTV SEVLGKAFVS FDKDIRQNYW PDSIRAQIAS LSAEDKSILQ
     GYADGMNAWI DKVNASPDKL LPQQFSTFGF KPKHWEPFDV AMIFVGTMAN RFSDSTSEID
     NLALLTAVKD KYGNDEGMAV FNQLKWLVNP SAPTTIAARE SSYPLKFDLQ NTQTAALLVP
     RYDQPAPMLD RPAKGTDGAL LAVTAIKNRE TIAAQFANGA NGLAGYPTTS NMWVIGKNKA
     QDAKAIMVNG PQFGWYAPAY TYGIGLHGAG YDVTGNTPFA YPGLVFGHNG TISWGSTAGF
     GDDVDIFAEK LSAEKPGYYQ HNGEWVKMLS RKETIAVKDG QPETFTVWRT LDGNVIKTDT
     RTQTAYAKAR AWAGKEVASL LAWTHQMKAK NWPEWTQQAA KQALTINWYY ADVNGNIGYV
     HTGAYPDRQP GHDPRLPVPD GKWDWKGLLS FDLNPKVYNP QSGYIANWNN SPQKDYPASD
     LFAFLWGGAD RVTEIDTILD KQPRFTADQA WDVIRQTSLR DLLRLFLPAL KDATANLAEN
     DPRRQLVDKL ASWDGENLVN DDGKTYQQPG SAILNAWLTS MLKRTVVAAV PAPFGKWYSA
     SGYETTQDGP TGSLNISVGA KILYEALQGD KSPIPQAVDL FGGKPEQEVI LAALDDAWQT
     LSKRYGNDVT GWKTPAMALT FRANNFFGVP QAAAKEARHQ AEYQNRGTEN DMIVFSPTSG
     NRPVLAWDVV APGQSGFIAP DGKADKHYDD QLKMYESFGR KSLWLTPQDV DEHKESQEVL
     QVQR