PAC_PRIMG
ID PAC_PRIMG Reviewed; 802 AA.
AC Q60136; Q9S463;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, 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 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=pga;
OS Priestia megaterium (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1404;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14945 / NBRC 13498 / 3781;
RA Kang J.H., Kim S.J., Park Y.C., Hwang Y., Yoo O.J., Kim Y.C.;
RT "Nucleotide sequence of the penicillin G acylase gene from Bacillus
RT megaterium and characteristics of the enzyme.";
RL Misainmurhag Hoiji 32:215-221(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14945 / NBRC 13498 / 3781;
RX PubMed=7875576; DOI=10.1016/0378-1097(94)00510-x;
RA Martin L.M., Prieto A.M., Cortes E., Garcia J.L.;
RT "Cloning and sequencing of the pac gene encoding the penicillin G acylase
RT of Bacillus megaterium ATCC 14945.";
RL FEMS Microbiol. Lett. 125:287-292(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CA4098;
RX PubMed=12114980;
RA Yang S., Huang Y.H., Huang X.D., Li S.Y., Yuan Z.Y.;
RT "High expression of penicillin G acylase gene from Bacillus megaterium in
RT Bacillus subtilis.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 31:601-603(1999).
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}.
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DR EMBL; U07682; AAB41343.1; -; Unassigned_DNA.
DR EMBL; Z37542; CAA85774.1; -; Genomic_DNA.
DR EMBL; AF161313; AAD45609.1; -; Genomic_DNA.
DR PIR; S49252; S49252.
DR PDB; 6NVW; X-ray; 2.20 A; A=25-234, B=266-802.
DR PDBsum; 6NVW; -.
DR AlphaFoldDB; Q60136; -.
DR SMR; Q60136; -.
DR MEROPS; S45.001; -.
DR BRENDA; 3.5.1.11; 656.
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 3D-structure; Antibiotic resistance; Calcium; Hydrolase; Metal-binding;
KW Secreted; Signal; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..802
FT /note="Penicillin G acylase"
FT /id="PRO_0000027341"
FT CHAIN 25..234
FT /note="Penicillin G acylase subunit alpha"
FT /id="PRO_0000027342"
FT PROPEP 235..265
FT /note="Spacer peptide"
FT /id="PRO_0000027343"
FT CHAIN 266..802
FT /note="Penicillin G acylase subunit beta"
FT /id="PRO_0000027344"
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"
FT VARIANT 3
FT /note="T -> M (in strain: CA4098)"
FT VARIANT 224
FT /note="D -> E (in strain: CA4098)"
FT VARIANT 232
FT /note="I -> K (in strain: CA4098)"
FT VARIANT 254
FT /note="T -> S (in strain: CA4098)"
FT VARIANT 349
FT /note="A -> T (in strain: CA4098)"
FT VARIANT 470
FT /note="S -> N (in strain: CA4098)"
FT VARIANT 524
FT /note="F -> Y (in strain: CA4098)"
FT VARIANT 569
FT /note="Q -> P (in strain: CA4098)"
FT VARIANT 586
FT /note="I -> A (in strain: CA4098)"
FT VARIANT 657
FT /note="N -> S (in strain: CA4098)"
FT VARIANT 740
FT /note="T -> K (in strain: CA4098)"
FT VARIANT 789..791
FT /note="NKA -> YKS (in strain: CA4098)"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 49..76
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 113..135
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 176..203
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:6NVW"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 296..304
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 321..334
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 340..348
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 365..374
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 378..389
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:6NVW"
FT TURN 400..403
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:6NVW"
FT TURN 411..414
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 416..428
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 432..441
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 495..500
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 504..510
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 520..525
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 533..541
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 547..559
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 562..577
FT /evidence="ECO:0007829|PDB:6NVW"
FT TURN 578..581
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 584..594
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 611..632
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 633..635
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 636..643
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 650..656
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 670..688
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 693..696
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 706..708
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 730..738
FT /evidence="ECO:0007829|PDB:6NVW"
FT STRAND 741..747
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 770..774
FT /evidence="ECO:0007829|PDB:6NVW"
FT HELIX 785..791
FT /evidence="ECO:0007829|PDB:6NVW"
SQ SEQUENCE 802 AA; 91988 MW; 877CA0564E50DFBD CRC64;
MKTKWLISVI ILFVFIFPQN LVFAGEDKNE GVKVVRDNFG VPHLYAKNKK DLYEAYGYVM
AKDRLFQLEM FRRGNEGTVS EIFGEDYLSK DEQSRRDGYS NKEIKKMIDG LDRQPKELIA
KFAEGISRYV NEALKDPDDK LSKEFHEYQF LPQKWTSTDV VRVYMVSMTY FMDNHQELKN
AEILAKLEHE YGTEVSRKMF DDLVWKNDPS APTSIVSEGK PKRDSSSQSL QILSSAVIKA
SEKVGKEREN FVQTSEELGL PLKIGSNAAI VGSEKSATGN ALLFSGPQVG FVAPGFLYEV
GLHAPGFDME GSGFIGYPFI MFGANNHFAL SATAGYGNVT DIFEEKLNAK NSSQYLYKGK
WRDMEKRKES FTVKGDNGEK KTVEKIYYRT VHGPVISRDE TNKVAYSKSW SFRGTEAQSM
SAYMKANWAK NLKEFENAAS EYTMSLNWYY ADKKGDIAYY HVGRYPVRNS KIDERIPTPG
TGEYEWKGFI PFKENPHVIN PKNGYVVNWN NKPSKEWVNG EYSFYWGEDN RVQQYINGME
ARGKVTLEDI NEINYTASFA QLRANLFKQL LIDVLDKNKS TNGNYIYLIE KLEEWNNLKE
DENKDGYYDA GIAAFFDEWW NNLHDKLFMD ELGDFYGITK EITDHRYGAS LAYKILNKES
TNYKWVNVDQ EKIIMESTNE VLAKLQSEKG LKAEKWRMPI KTMTFGEKSL IGIPHGYGSM
TPIIEMNRGS ENHYIEMTPT GPSGFNITPP GQIGFVKKDG TISDHYDDQL VMFAEWKFKP
YLFNKKDINK AAKNVSALNM SK
