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Penicillin G acylase (EC 3.5.1.11) (Penicillin G amidase) (Penicillin G amidohydrolase) [Cleaved into: Penicillin G acylase subunit alpha; Penicillin G acylase subunit beta]

 PAC_ECOLX               Reviewed;         846 AA.
P06875; Q47434; Q47435; Q47436; Q47437; Q60253;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 2.
28-MAR-2018, entry version 127.
RecName: Full=Penicillin G acylase;
EC=3.5.1.11;
AltName: Full=Penicillin G amidase;
AltName: Full=Penicillin G amidohydrolase;
Contains:
RecName: Full=Penicillin G acylase subunit alpha;
Contains:
RecName: Full=Penicillin G acylase subunit beta;
Flags: Precursor;
Name=pac;
Escherichia coli.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=562;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3016663; DOI=10.1093/nar/14.14.5713;
Schumacher G., Sizmann D., Haug H., Buckel P., Boeck A.;
"Penicillin acylase from E. coli: unique gene-protein relation.";
Nucleic Acids Res. 14:5713-5727(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3315861; DOI=10.1016/0378-1119(87)90161-2;
Oh S.-J., Kim Y.-C., Park Y.-W., Min S.-Y., Kim I.-S., Kang H.-S.;
"Complete nucleotide sequence of the penicillin G acylase gene and the
flanking regions, and its expression in Escherichia coli.";
Gene 56:87-97(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-368.
STRAIN=W / ATCC 11105 / DSM 1900;
PubMed=3005131; DOI=10.1016/0378-1119(85)90018-6;
Oliver G., Valle F., Rosetti F., Gomez-Pedrozo M., Santamaria P.,
Gosset G., Bolivar F.;
"A common precursor for the two subunits of the penicillin acylase
from Escherichia coli ATCC11105.";
Gene 40:9-14(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-368.
PubMed=3556321; DOI=10.1016/0378-1119(86)90316-1;
Valle F., Gosset G., Tenorio B., Oliver G., Bolivar F.;
"Characterization of the regulatory region of the Escherichia coli
penicillin acylase structural gene.";
Gene 50:119-122(1986).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-350 AND 741-846.
PubMed=2989404;
Bruns W., Hoppe J., Tsai H., Bruning H.J., Maywald F., Collins J.,
Mayer H.;
"Structure of the penicillin acylase gene from Escherichia coli: a
periplasmic enzyme that undergoes multiple proteolytic processing.";
J. Mol. Appl. Genet. 3:36-44(1985).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
STRAIN=W / ATCC 11105 / DSM 1900;
Radoja S., Francetic O., Stojicevic N., Moric I., Glisin S.,
Konstantinovic M.;
"Transcriptional and gene fusion analyses of the Escherichia coli
penicillin amidase gene expression.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 27-36 AND 291-299.
STRAIN=W / ATCC 11105 / DSM 1900;
PubMed=1849824; DOI=10.1111/j.1432-1033.1991.tb15884.x;
Slade A., Horrocks A.J., Lindsay C.D., Dunbar B., Virden R.;
"Site-directed chemical conversion of serine to cysteine in penicillin
acylase from Escherichia coli ATCC 11105. Effect on conformation and
catalytic activity.";
Eur. J. Biochem. 197:75-80(1991).
[8]
PROTEOLYTIC PROCESSING.
PubMed=2205499; DOI=10.1111/j.1432-1033.1990.tb19207.x;
Sizmann D., Keilmann C., Boeck A.;
"Primary structure requirements for the maturation in vivo of
penicillin acylase from Escherichia coli ATCC 11105.";
Eur. J. Biochem. 192:143-151(1990).
[9]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND MUTAGENESIS OF SER-290.
STRAIN=W / ATCC 11105 / DSM 1900;
PubMed=7816145; DOI=10.1038/373264a0;
Duggleby H.J., Tolley S.P., Hill C.P., Dodson E.J., Dodson G.,
Moody P.C.E.;
"Penicillin acylase has a single-amino-acid catalytic centre.";
Nature 373:264-268(1995).
[10]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 27-235.
PubMed=11601852; DOI=10.1006/jmbi.2001.5043;
McVey C.E., Walsh M.A., Dodson G.G., Wilson K.S., Brannigan J.A.;
"Crystal structures of penicillin acylase enzyme-substrate complexes:
structural insights into the catalytic mechanism.";
J. Mol. Biol. 313:139-150(2001).
-!- CATALYTIC ACTIVITY: Penicillin + H(2)O = a carboxylate + 6-
aminopenicillanate.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 1 Ca(2+) ion per dimer.;
-!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit
processed from the same precursor.
-!- SUBCELLULAR LOCATION: Periplasm.
-!- SIMILARITY: Belongs to the peptidase S45 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M15950; AAA24269.1; -; Genomic_DNA.
EMBL; X04114; CAA27728.1; -; Genomic_DNA.
EMBL; M17609; AAA24324.1; -; Genomic_DNA.
EMBL; M14424; AAA24270.1; -; Genomic_DNA.
EMBL; M11672; AAA24258.1; -; Genomic_DNA.
EMBL; M12373; AAA24259.1; -; Genomic_DNA.
EMBL; AF109125; AAD19653.1; -; Genomic_DNA.
PIR; A23593; PNECA.
RefSeq; WP_000797400.1; NZ_PJDB01000025.1.
PDB; 1AI4; X-ray; 2.35 A; A=27-235, B=290-846.
PDB; 1AI5; X-ray; 2.36 A; A=27-235, B=290-846.
PDB; 1AI6; X-ray; 2.55 A; A=27-235, B=290-846.
PDB; 1AI7; X-ray; 2.50 A; A=27-235, B=290-846.
PDB; 1AJN; X-ray; 2.36 A; A=27-235, B=290-846.
PDB; 1AJP; X-ray; 2.31 A; A=27-235, B=290-846.
PDB; 1AJQ; X-ray; 2.05 A; A=27-235, B=290-846.
PDB; 1E3A; X-ray; 1.80 A; A=27-286, B=287-846.
PDB; 1FXH; X-ray; 1.97 A; A=27-235, B=290-846.
PDB; 1FXV; X-ray; 2.25 A; A=27-235, B=290-846.
PDB; 1GK9; X-ray; 1.30 A; A=27-286, B=290-846.
PDB; 1GKF; X-ray; 1.41 A; A=27-286, B=290-846.
PDB; 1GM7; X-ray; 1.45 A; A=27-235, B=290-846.
PDB; 1GM8; X-ray; 2.00 A; A=27-235, B=290-846.
PDB; 1GM9; X-ray; 1.80 A; A=27-235, B=290-846.
PDB; 1H2G; X-ray; 2.00 A; A=27-235, B=290-846.
PDB; 1JX9; X-ray; 2.28 A; A=26-234, B=290-846.
PDB; 1K5Q; X-ray; 2.34 A; A=26-234, B=290-846.
PDB; 1K5S; X-ray; 2.43 A; A=26-234, B=290-846.
PDB; 1K7D; X-ray; 2.15 A; A=26-234, B=290-846.
PDB; 1KEC; X-ray; 2.30 A; A=26-234, B=290-846.
PDB; 1PNK; X-ray; 1.90 A; A=27-235, B=290-846.
PDB; 1PNL; X-ray; 2.50 A; A=27-235, B=290-846.
PDB; 1PNM; X-ray; 2.50 A; A=27-235, B=290-846.
PDBsum; 1AI4; -.
PDBsum; 1AI5; -.
PDBsum; 1AI6; -.
PDBsum; 1AI7; -.
PDBsum; 1AJN; -.
PDBsum; 1AJP; -.
PDBsum; 1AJQ; -.
PDBsum; 1E3A; -.
PDBsum; 1FXH; -.
PDBsum; 1FXV; -.
PDBsum; 1GK9; -.
PDBsum; 1GKF; -.
PDBsum; 1GM7; -.
PDBsum; 1GM8; -.
PDBsum; 1GM9; -.
PDBsum; 1H2G; -.
PDBsum; 1JX9; -.
PDBsum; 1K5Q; -.
PDBsum; 1K5S; -.
PDBsum; 1K7D; -.
PDBsum; 1KEC; -.
PDBsum; 1PNK; -.
PDBsum; 1PNL; -.
PDBsum; 1PNM; -.
ProteinModelPortal; P06875; -.
SMR; P06875; -.
DrugBank; DB08193; 2-(3-NITROPHENYL)ACETIC ACID.
DrugBank; DB07331; 2-(4-NITROPHENYL)ACETIC ACID.
MEROPS; S45.001; -.
PRIDE; P06875; -.
BioCyc; MetaCyc:MONOMER-18775; -.
BRENDA; 3.5.1.11; 2026.
SABIO-RK; P06875; -.
EvolutionaryTrace; P06875; -.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008953; F:penicillin amidase activity; IEA:UniProtKB-EC.
GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
CDD; cd03748; Ntn_PGA; 1.
Gene3D; 1.10.439.10; -; 1.
Gene3D; 3.60.20.10; -; 3.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR014395; Pen/GL7ACA/AHL_acylase.
InterPro; IPR023343; Penicillin_amidase_dom1.
InterPro; IPR033813; PGA_C.
InterPro; IPR002692; S45.
PANTHER; PTHR34218; PTHR34218; 1.
Pfam; PF01804; Penicil_amidase; 1.
PIRSF; PIRSF001227; Pen_acylase; 1.
SUPFAM; SSF56235; SSF56235; 2.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Calcium;
Direct protein sequencing; Hydrolase; Metal-binding; Periplasm;
Signal; Zymogen.
SIGNAL 1 26 {ECO:0000269|PubMed:1849824}.
CHAIN 27 846 Penicillin G acylase.
/FTId=PRO_0000027345.
CHAIN 27 235 Penicillin G acylase subunit alpha.
/FTId=PRO_0000027346.
PROPEP 236 289 Spacer peptide.
/FTId=PRO_0000027347.
CHAIN 290 846 Penicillin G acylase subunit beta.
/FTId=PRO_0000027348.
ACT_SITE 290 290 Nucleophile.
METAL 178 178 Calcium.
METAL 362 362 Calcium.
METAL 364 364 Calcium; via carbonyl oxygen.
METAL 365 365 Calcium.
METAL 494 494 Calcium; via carbonyl oxygen.
METAL 541 541 Calcium.
MUTAGEN 290 290 S->C: Loss of activity.
{ECO:0000269|PubMed:7816145}.
CONFLICT 68 68 Q -> R (in Ref. 5; AAA24258).
{ECO:0000305}.
CONFLICT 77 77 Q -> R (in Ref. 5; AAA24258).
{ECO:0000305}.
CONFLICT 97 97 R -> S (in Ref. 5; AAA24258).
{ECO:0000305}.
CONFLICT 103 103 A -> R (in Ref. 3; AAA24270).
{ECO:0000305}.
CONFLICT 130 130 I -> T (in Ref. 2 and 5). {ECO:0000305}.
CONFLICT 217 217 A -> G (in Ref. 5; AAA24258).
{ECO:0000305}.
CONFLICT 250 250 R -> P (in Ref. 3; AAA24270).
{ECO:0000305}.
CONFLICT 272 272 A -> V (in Ref. 1 and 5). {ECO:0000305}.
CONFLICT 305 305 A -> R (in Ref. 3; AAA24270).
{ECO:0000305}.
CONFLICT 342 350 PGLVFGHNG -> LGWFPGYMV (in Ref. 5;
AAA24258). {ECO:0000305}.
CONFLICT 632 632 G -> P (in Ref. 2; AAA24324).
{ECO:0000305}.
CONFLICT 789 789 W -> Q (in Ref. 5; AAA24259).
{ECO:0000305}.
STRAND 32 38 {ECO:0000244|PDB:1GK9}.
STRAND 43 46 {ECO:0000244|PDB:1GK9}.
HELIX 50 77 {ECO:0000244|PDB:1GK9}.
HELIX 81 84 {ECO:0000244|PDB:1GK9}.
HELIX 86 88 {ECO:0000244|PDB:1GK9}.
HELIX 89 97 {ECO:0000244|PDB:1GK9}.
HELIX 101 109 {ECO:0000244|PDB:1GK9}.
HELIX 113 135 {ECO:0000244|PDB:1GK9}.
HELIX 137 140 {ECO:0000244|PDB:1GK9}.
HELIX 143 148 {ECO:0000244|PDB:1GK9}.
HELIX 157 167 {ECO:0000244|PDB:1GK9}.
HELIX 169 172 {ECO:0000244|PDB:1GK9}.
HELIX 178 192 {ECO:0000244|PDB:1GK9}.
HELIX 194 204 {ECO:0000244|PDB:1GK9}.
STRAND 214 216 {ECO:0000244|PDB:1GK9}.
TURN 218 220 {ECO:0000244|PDB:1GK9}.
HELIX 229 231 {ECO:0000244|PDB:1E3A}.
HELIX 232 234 {ECO:0000244|PDB:1GK9}.
HELIX 235 237 {ECO:0000244|PDB:1E3A}.
HELIX 246 249 {ECO:0000244|PDB:1E3A}.
HELIX 264 278 {ECO:0000244|PDB:1E3A}.
HELIX 279 281 {ECO:0000244|PDB:1E3A}.
STRAND 291 295 {ECO:0000244|PDB:1GK9}.
TURN 297 299 {ECO:0000244|PDB:1GK9}.
STRAND 300 310 {ECO:0000244|PDB:1GK9}.
STRAND 316 318 {ECO:0000244|PDB:1GK9}.
STRAND 320 328 {ECO:0000244|PDB:1GK9}.
STRAND 331 338 {ECO:0000244|PDB:1GK9}.
STRAND 345 348 {ECO:0000244|PDB:1GK9}.
STRAND 350 358 {ECO:0000244|PDB:1GK9}.
STRAND 364 370 {ECO:0000244|PDB:1GK9}.
STRAND 373 375 {ECO:0000244|PDB:1PNK}.
STRAND 378 381 {ECO:0000244|PDB:1GK9}.
STRAND 384 387 {ECO:0000244|PDB:1GK9}.
STRAND 389 395 {ECO:0000244|PDB:1GK9}.
STRAND 403 410 {ECO:0000244|PDB:1GK9}.
STRAND 413 419 {ECO:0000244|PDB:1GK9}.
TURN 420 423 {ECO:0000244|PDB:1GK9}.
STRAND 424 430 {ECO:0000244|PDB:1GK9}.
TURN 431 434 {ECO:0000244|PDB:1GK9}.
HELIX 436 445 {ECO:0000244|PDB:1GK9}.
HELIX 446 448 {ECO:0000244|PDB:1GK9}.
HELIX 452 459 {ECO:0000244|PDB:1GK9}.
STRAND 464 472 {ECO:0000244|PDB:1GK9}.
STRAND 477 483 {ECO:0000244|PDB:1GK9}.
STRAND 498 502 {ECO:0000244|PDB:1GK9}.
HELIX 512 514 {ECO:0000244|PDB:1GK9}.
STRAND 517 520 {ECO:0000244|PDB:1GK9}.
STRAND 524 530 {ECO:0000244|PDB:1GK9}.
STRAND 532 534 {ECO:0000244|PDB:1GK9}.
HELIX 553 561 {ECO:0000244|PDB:1GK9}.
STRAND 562 564 {ECO:0000244|PDB:1GK9}.
HELIX 568 580 {ECO:0000244|PDB:1GK9}.
HELIX 585 596 {ECO:0000244|PDB:1GK9}.
HELIX 604 613 {ECO:0000244|PDB:1GK9}.
STRAND 625 630 {ECO:0000244|PDB:1GK9}.
HELIX 632 646 {ECO:0000244|PDB:1GK9}.
HELIX 648 651 {ECO:0000244|PDB:1GK9}.
HELIX 656 660 {ECO:0000244|PDB:1GK9}.
HELIX 680 689 {ECO:0000244|PDB:1GK9}.
HELIX 690 693 {ECO:0000244|PDB:1GK9}.
STRAND 694 696 {ECO:0000244|PDB:1E3A}.
TURN 702 705 {ECO:0000244|PDB:1GK9}.
HELIX 708 727 {ECO:0000244|PDB:1GK9}.
HELIX 731 733 {ECO:0000244|PDB:1GK9}.
STRAND 741 746 {ECO:0000244|PDB:1GK9}.
STRAND 752 754 {ECO:0000244|PDB:1GK9}.
HELIX 756 758 {ECO:0000244|PDB:1GK9}.
STRAND 760 764 {ECO:0000244|PDB:1GK9}.
STRAND 770 778 {ECO:0000244|PDB:1GK9}.
STRAND 780 783 {ECO:0000244|PDB:1GM8}.
STRAND 785 791 {ECO:0000244|PDB:1GK9}.
STRAND 810 813 {ECO:0000244|PDB:1AI4}.
HELIX 814 818 {ECO:0000244|PDB:1GK9}.
STRAND 823 825 {ECO:0000244|PDB:1K7D}.
HELIX 829 834 {ECO:0000244|PDB:1GK9}.
STRAND 836 843 {ECO:0000244|PDB:1GK9}.
SEQUENCE 846 AA; 94643 MW; 48570EDCB53BA227 CRC64;
MKNRNRMIVN CVTASLMYYW SLPALAEQSS SEIKIVRDEY GMPHIYANDT WHLFYGYGYV
VAQDRLFQME MARRSTQGTV AEVLGKDFVK FDKDIRRNYW PDAIRAQIAA LSPEDMSILQ
GYADGMNAWI DKVNTNPETL LPKQFNTFGF TPKRWEPFDV AMIFVGTMAN RFSDSTSEID
NLALLTALKD KYGVSQGMAV FNQLKWLVNP SAPTTIAVQE SNYPLKFNQQ NSQTAALLPR
YDLPAPMLDR PAKGADGALL ALTAGKNRET IAAQFAQGGA NGLAGYPTTS NMWVIGKSKA
QDAKAIMVNG PQFGWYAPAY TYGIGLHGAG YDVTGNTPFA YPGLVFGHNG VISWGSTAGF
GDDVDIFAER LSAEKPGYYL HNGKWVKMLS REETITVKNG QAETFTVWRT VHGNILQTDQ
TTQTAYAKSR AWDGKEVASL LAWTHQMKAK NWQEWTQQAA KQALTINWYY ADVNGNIGYV
HTGAYPDRQS GHDPRLPVPG TGKWDWKGLL PFEMNPKVYN PQSGYIANWN NSPQKDYPAS
DLFAFLWGGA DRVTEIDRLL EQKPRLTADQ AWDVIRQTSR QDLNLRLFLP TLQAATSGLT
QSDPRRQLVE TLTRWDGINL LNDDGKTWQQ PGSAILNVWL TSMLKRTVVA AVPMPFDKWY
SASGYETTQD GPTGSLNISV GAKILYEAVQ GDKSPIPQAV DLFAGKPQQE VVLAALEDTW
ETLSKRYGNN VSNWKTPAMA LTFRANNFFG VPQAAAEETR HQAEYQNRGT ENDMIVFSPT
TSDRPVLAWD VVAPGQSGFI APDGTVDKHY EDQLKMYENF GRKSLWLTKQ DVEAHKESQE
VLHVQR


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