ID   PAC_RHIVS               Reviewed;         802 AA.
AC   P31956;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Penicillin G acylase;
DE            EC=3.5.1.11;
DE   AltName: Full=Penicillin G amidase;
DE   AltName: Full=Penicillin G 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; Synonyms=pa;
OS   Rhizobium viscosum (Arthrobacter viscosus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=1673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15294 / DSM 20159 / IFO 13497 / LMG 16186 / NCIMB 10268;
RX   PubMed=8200542; DOI=10.1016/0378-1119(94)90608-4;
RA   Konstantinovic M., Marjanovic N., Ljubijankic G., Glisin V.;
RT   "The penicillin amidase of Arthrobacter viscosus (ATCC 15294).";
RL   Gene 143:79-83(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 27-67 AND 266-303.
RC   STRAIN=ATCC 15294 / DSM 20159 / IFO 13497 / LMG 16186 / NCIMB 10268;
RX   PubMed=3214149; DOI=10.1128/aem.54.11.2603-2607.1988;
RA   Ohashi H., Katsuta Y., Hashizume T., Abe S.N., Kajiura H., Hattori H.,
RA   Kamei T., Yano M.;
RT   "Molecular cloning of the penicillin G acylase gene from Arthrobacter
RT   viscosus.";
RL   Appl. Environ. Microbiol. 54:2603-2607(1988).
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:0000305};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305};
CC   -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit processed
CC       from the same precursor. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S45 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; L04471; AAA22077.1; -; Genomic_DNA.
DR   PIR; I39665; I39665.
DR   AlphaFoldDB; P31956; -.
DR   SMR; P31956; -.
DR   MEROPS; S45.001; -.
DR   BRENDA; 3.5.1.11; 461.
DR   GO; GO:0005576; C:extracellular region; 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   Antibiotic resistance; Calcium; Direct protein sequencing; Hydrolase;
KW   Metal-binding; Secreted; Signal; Zymogen.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:3214149"
FT   CHAIN           27..802
FT                   /note="Penicillin G acylase"
FT                   /id="PRO_0000027337"
FT   CHAIN           27..234
FT                   /note="Penicillin G acylase subunit alpha"
FT                   /id="PRO_0000027338"
FT   PROPEP          235..265
FT                   /note="Spacer peptide"
FT                   /evidence="ECO:0000269|PubMed:3214149"
FT                   /id="PRO_0000027339"
FT   CHAIN           266..802
FT                   /note="Penicillin G acylase subunit beta"
FT                   /id="PRO_0000027340"
FT   ACT_SITE        266
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255"
FT   BINDING         341
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   802 AA;  92113 MW;  9863E58C526C85D7 CRC64;
     MKMKWLISVI ILFVFIFPQN LVFAGEDKNE GVKVVRDNFG VPHLYAKNKK DLYEAYGYVM
     AKDRLFQLEM FRRGNEGTVS EIFGEDYLSK DEQSRRDGYS NKEIKKMIDG LDRQPRELIA
     KFAEGISRYV NEALKDPDDK LSKEFHEYQF LPQKWTSTDV VRVYMVSMTY LWIITRELKN
     AEILAKLEHE YGTEVSRKMF DDLVWKNDPS APTSIVSEGK PKRESSSQSL QKLSSAVIKA
     SEKVGKEREN FVQSSEELGL PLKIGSNAAI VGSEKSATGN ALLFSGPQVG FVAPGFLYEV
     GLHAPGFDME GSGFIGYPFI MFGANNHFAL SATAGYGNVT DIFEEKLNTK NSSQYLYKGK
     WRDMEKRKES FTVKGDNGEK KTVEKIYYRT VHGPVISRDE TNKVAYSKYV SFRGTEAQSM
     SAYMKANWAK NLKEFENAAS EYTMSLNWYY ADKKGDIAYY HVGRYPVRNN KIDERIPTPG
     TGEYEWKGFI PFKENPHVIN PKNGYVVNWN NKPSKEWVNG EYSYYWGEDN RVQQYINGME
     ARGKVTLEDI NEINYTASFA QLRANLFKPL LIDVLDKNKS TNGNYTYLIE KLEEWNNLKE
     DENKDGYYDA GIAAFFDEWW NNLHDKLFMD ELGDFYGITK EITDHRYGAS LAYKNISKES
     TNYKWVNVDQ EKIIMESTNE VLAKLQSEKG LKAEKWRMPI KTMTFGEKSL IGIPHGYGSM
     TPIIEMNRGS ENHYIEMTPK GPSGFNITPP GQIGFVKKDG TISDHYDDQL VMFAEWKFKP
     YLFNKKDIYK AATNVSALNM SK