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Protein

Penicillin G acylase

Gene

pac

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Penicillin + H2O = a carboxylate + 6-aminopenicillanate.

Cofactori

Ca2+Note: Binds 1 Ca2+ ion per dimer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi178 – 1781Calcium
Active sitei290 – 2901Nucleophile
Metal bindingi362 – 3621Calcium
Metal bindingi364 – 3641Calcium; via carbonyl oxygen
Metal bindingi365 – 3651Calcium
Metal bindingi494 – 4941Calcium; via carbonyl oxygen
Metal bindingi541 – 5411Calcium

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.5.1.11. 2026.
SABIO-RKP06875.

Protein family/group databases

MEROPSiS45.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Penicillin G acylase (EC:3.5.1.11)
Alternative name(s):
Penicillin G amidase
Penicillin G amidohydrolase
Cleaved into the following 2 chains:
Gene namesi
Name:pac
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi290 – 2901S → C: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 846820Penicillin G acylasePRO_0000027345Add
BLAST
Chaini27 – 235209Penicillin G acylase subunit alphaPRO_0000027346Add
BLAST
Propeptidei236 – 28954Spacer peptidePRO_0000027347Add
BLAST
Chaini290 – 846557Penicillin G acylase subunit betaPRO_0000027348Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

PRIDEiP06875.

Interactioni

Subunit structurei

Heterodimer of an alpha subunit and a beta subunit processed from the same precursor.

Structurei

Secondary structure

1
846
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 387Combined sources
Beta strandi43 – 464Combined sources
Helixi50 – 7728Combined sources
Helixi81 – 844Combined sources
Helixi86 – 883Combined sources
Helixi89 – 979Combined sources
Helixi101 – 1099Combined sources
Helixi113 – 13523Combined sources
Helixi137 – 1404Combined sources
Helixi143 – 1486Combined sources
Helixi157 – 16711Combined sources
Helixi169 – 1724Combined sources
Helixi178 – 19215Combined sources
Helixi194 – 20411Combined sources
Beta strandi214 – 2163Combined sources
Turni218 – 2203Combined sources
Helixi229 – 2313Combined sources
Helixi232 – 2343Combined sources
Helixi235 – 2373Combined sources
Helixi246 – 2494Combined sources
Helixi264 – 27815Combined sources
Helixi279 – 2813Combined sources
Beta strandi291 – 2955Combined sources
Turni297 – 2993Combined sources
Beta strandi300 – 31011Combined sources
Beta strandi316 – 3183Combined sources
Beta strandi320 – 3289Combined sources
Beta strandi331 – 3388Combined sources
Beta strandi345 – 3484Combined sources
Beta strandi350 – 3589Combined sources
Beta strandi364 – 3707Combined sources
Beta strandi373 – 3753Combined sources
Beta strandi378 – 3814Combined sources
Beta strandi384 – 3874Combined sources
Beta strandi389 – 3957Combined sources
Beta strandi403 – 4108Combined sources
Beta strandi413 – 4197Combined sources
Turni420 – 4234Combined sources
Beta strandi424 – 4307Combined sources
Turni431 – 4344Combined sources
Helixi436 – 44510Combined sources
Helixi446 – 4483Combined sources
Helixi452 – 4598Combined sources
Beta strandi464 – 4729Combined sources
Beta strandi477 – 4837Combined sources
Beta strandi498 – 5025Combined sources
Helixi512 – 5143Combined sources
Beta strandi517 – 5204Combined sources
Beta strandi524 – 5307Combined sources
Beta strandi532 – 5343Combined sources
Helixi553 – 5619Combined sources
Beta strandi562 – 5643Combined sources
Helixi568 – 58013Combined sources
Helixi585 – 59612Combined sources
Helixi604 – 61310Combined sources
Beta strandi625 – 6306Combined sources
Helixi632 – 64615Combined sources
Helixi648 – 6514Combined sources
Helixi656 – 6605Combined sources
Helixi680 – 68910Combined sources
Helixi690 – 6934Combined sources
Beta strandi694 – 6963Combined sources
Turni702 – 7054Combined sources
Helixi708 – 72720Combined sources
Helixi731 – 7333Combined sources
Beta strandi741 – 7466Combined sources
Beta strandi752 – 7543Combined sources
Helixi756 – 7583Combined sources
Beta strandi760 – 7645Combined sources
Beta strandi770 – 7789Combined sources
Beta strandi780 – 7834Combined sources
Beta strandi785 – 7917Combined sources
Beta strandi810 – 8134Combined sources
Helixi814 – 8185Combined sources
Beta strandi823 – 8253Combined sources
Helixi829 – 8346Combined sources
Beta strandi836 – 8438Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AI4X-ray2.35A27-235[»]
B290-846[»]
1AI5X-ray2.36A27-235[»]
B290-846[»]
1AI6X-ray2.55A27-235[»]
B290-846[»]
1AI7X-ray2.50A27-235[»]
B290-846[»]
1AJNX-ray2.36A27-235[»]
B290-846[»]
1AJPX-ray2.31A27-235[»]
B290-846[»]
1AJQX-ray2.05A27-235[»]
B290-846[»]
1E3AX-ray1.80A27-286[»]
B287-846[»]
1FXHX-ray1.97A27-235[»]
B290-846[»]
1FXVX-ray2.25A27-235[»]
B290-846[»]
1GK9X-ray1.30A27-286[»]
B290-846[»]
1GKFX-ray1.41A27-286[»]
B290-846[»]
1GM7X-ray1.45A27-235[»]
B290-846[»]
1GM8X-ray2.00A27-235[»]
B290-846[»]
1GM9X-ray1.80A27-235[»]
B290-846[»]
1H2GX-ray2.00A27-235[»]
B290-846[»]
1JX9X-ray2.28A26-234[»]
B290-846[»]
1K5QX-ray2.34A26-234[»]
B290-846[»]
1K5SX-ray2.43A26-234[»]
B290-846[»]
1K7DX-ray2.15A26-234[»]
B290-846[»]
1KECX-ray2.30A26-234[»]
B290-846[»]
1PNKX-ray1.90A27-235[»]
B290-846[»]
1PNLX-ray2.50A27-235[»]
B290-846[»]
1PNMX-ray2.50A27-235[»]
B290-846[»]
ProteinModelPortaliP06875.
SMRiP06875. Positions 28-286, 290-846.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06875.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S45 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.10.439.10. 1 hit.
3.60.20.10. 2 hits.
InterProiIPR029055. Ntn_hydrolases_N.
IPR002692. Pen/cephal_acylase.
IPR014395. Pen_acylase.
IPR023343. Penicillin_amidase_dom1.
[Graphical view]
PfamiPF01804. Penicil_amidase. 1 hit.
[Graphical view]
PIRSFiPIRSF001227. Pen_acylase. 1 hit.
SUPFAMiSSF56235. SSF56235. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06875-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNRNRMIVN CVTASLMYYW SLPALAEQSS SEIKIVRDEY GMPHIYANDT
60 70 80 90 100
WHLFYGYGYV VAQDRLFQME MARRSTQGTV AEVLGKDFVK FDKDIRRNYW
110 120 130 140 150
PDAIRAQIAA LSPEDMSILQ GYADGMNAWI DKVNTNPETL LPKQFNTFGF
160 170 180 190 200
TPKRWEPFDV AMIFVGTMAN RFSDSTSEID NLALLTALKD KYGVSQGMAV
210 220 230 240 250
FNQLKWLVNP SAPTTIAVQE SNYPLKFNQQ NSQTAALLPR YDLPAPMLDR
260 270 280 290 300
PAKGADGALL ALTAGKNRET IAAQFAQGGA NGLAGYPTTS NMWVIGKSKA
310 320 330 340 350
QDAKAIMVNG PQFGWYAPAY TYGIGLHGAG YDVTGNTPFA YPGLVFGHNG
360 370 380 390 400
VISWGSTAGF GDDVDIFAER LSAEKPGYYL HNGKWVKMLS REETITVKNG
410 420 430 440 450
QAETFTVWRT VHGNILQTDQ TTQTAYAKSR AWDGKEVASL LAWTHQMKAK
460 470 480 490 500
NWQEWTQQAA KQALTINWYY ADVNGNIGYV HTGAYPDRQS GHDPRLPVPG
510 520 530 540 550
TGKWDWKGLL PFEMNPKVYN PQSGYIANWN NSPQKDYPAS DLFAFLWGGA
560 570 580 590 600
DRVTEIDRLL EQKPRLTADQ AWDVIRQTSR QDLNLRLFLP TLQAATSGLT
610 620 630 640 650
QSDPRRQLVE TLTRWDGINL LNDDGKTWQQ PGSAILNVWL TSMLKRTVVA
660 670 680 690 700
AVPMPFDKWY SASGYETTQD GPTGSLNISV GAKILYEAVQ GDKSPIPQAV
710 720 730 740 750
DLFAGKPQQE VVLAALEDTW ETLSKRYGNN VSNWKTPAMA LTFRANNFFG
760 770 780 790 800
VPQAAAEETR HQAEYQNRGT ENDMIVFSPT TSDRPVLAWD VVAPGQSGFI
810 820 830 840
APDGTVDKHY EDQLKMYENF GRKSLWLTKQ DVEAHKESQE VLHVQR
Length:846
Mass (Da):94,643
Last modified:July 1, 1989 - v2
Checksum:i48570EDCB53BA227
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681Q → R in AAA24258 (PubMed:2989404).Curated
Sequence conflicti77 – 771Q → R in AAA24258 (PubMed:2989404).Curated
Sequence conflicti97 – 971R → S in AAA24258 (PubMed:2989404).Curated
Sequence conflicti103 – 1031A → R in AAA24270 (PubMed:3005131).Curated
Sequence conflicti130 – 1301I → T (PubMed:3315861).Curated
Sequence conflicti130 – 1301I → T (PubMed:2989404).Curated
Sequence conflicti217 – 2171A → G in AAA24258 (PubMed:2989404).Curated
Sequence conflicti250 – 2501R → P in AAA24270 (PubMed:3005131).Curated
Sequence conflicti272 – 2721A → V (PubMed:3016663).Curated
Sequence conflicti272 – 2721A → V (PubMed:2989404).Curated
Sequence conflicti305 – 3051A → R in AAA24270 (PubMed:3005131).Curated
Sequence conflicti342 – 3509PGLVFGHNG → LGWFPGYMV in AAA24258 (PubMed:2989404).Curated
Sequence conflicti632 – 6321G → P in AAA24324 (PubMed:3315861).Curated
Sequence conflicti789 – 7891W → Q in AAA24259 (PubMed:2989404).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15950 Genomic DNA. Translation: AAA24269.1.
X04114 Genomic DNA. Translation: CAA27728.1.
M17609 Genomic DNA. Translation: AAA24324.1.
M14424 Genomic DNA. Translation: AAA24270.1.
M11672 Genomic DNA. Translation: AAA24258.1.
M12373 Genomic DNA. Translation: AAA24259.1.
AF109125 Genomic DNA. Translation: AAD19653.1.
PIRiA23593. PNECA.
RefSeqiWP_000797400.1. NZ_LQUA01000035.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15950 Genomic DNA. Translation: AAA24269.1.
X04114 Genomic DNA. Translation: CAA27728.1.
M17609 Genomic DNA. Translation: AAA24324.1.
M14424 Genomic DNA. Translation: AAA24270.1.
M11672 Genomic DNA. Translation: AAA24258.1.
M12373 Genomic DNA. Translation: AAA24259.1.
AF109125 Genomic DNA. Translation: AAD19653.1.
PIRiA23593. PNECA.
RefSeqiWP_000797400.1. NZ_LQUA01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AI4X-ray2.35A27-235[»]
B290-846[»]
1AI5X-ray2.36A27-235[»]
B290-846[»]
1AI6X-ray2.55A27-235[»]
B290-846[»]
1AI7X-ray2.50A27-235[»]
B290-846[»]
1AJNX-ray2.36A27-235[»]
B290-846[»]
1AJPX-ray2.31A27-235[»]
B290-846[»]
1AJQX-ray2.05A27-235[»]
B290-846[»]
1E3AX-ray1.80A27-286[»]
B287-846[»]
1FXHX-ray1.97A27-235[»]
B290-846[»]
1FXVX-ray2.25A27-235[»]
B290-846[»]
1GK9X-ray1.30A27-286[»]
B290-846[»]
1GKFX-ray1.41A27-286[»]
B290-846[»]
1GM7X-ray1.45A27-235[»]
B290-846[»]
1GM8X-ray2.00A27-235[»]
B290-846[»]
1GM9X-ray1.80A27-235[»]
B290-846[»]
1H2GX-ray2.00A27-235[»]
B290-846[»]
1JX9X-ray2.28A26-234[»]
B290-846[»]
1K5QX-ray2.34A26-234[»]
B290-846[»]
1K5SX-ray2.43A26-234[»]
B290-846[»]
1K7DX-ray2.15A26-234[»]
B290-846[»]
1KECX-ray2.30A26-234[»]
B290-846[»]
1PNKX-ray1.90A27-235[»]
B290-846[»]
1PNLX-ray2.50A27-235[»]
B290-846[»]
1PNMX-ray2.50A27-235[»]
B290-846[»]
ProteinModelPortaliP06875.
SMRiP06875. Positions 28-286, 290-846.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS45.001.

Proteomic databases

PRIDEiP06875.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.5.1.11. 2026.
SABIO-RKP06875.

Miscellaneous databases

EvolutionaryTraceiP06875.

Family and domain databases

Gene3Di1.10.439.10. 1 hit.
3.60.20.10. 2 hits.
InterProiIPR029055. Ntn_hydrolases_N.
IPR002692. Pen/cephal_acylase.
IPR014395. Pen_acylase.
IPR023343. Penicillin_amidase_dom1.
[Graphical view]
PfamiPF01804. Penicil_amidase. 1 hit.
[Graphical view]
PIRSFiPIRSF001227. Pen_acylase. 1 hit.
SUPFAMiSSF56235. SSF56235. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Penicillin acylase from E. coli: unique gene-protein relation."
    Schumacher G., Sizmann D., Haug H., Buckel P., Boeck A.
    Nucleic Acids Res. 14:5713-5727(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete nucleotide sequence of the penicillin G acylase gene and the flanking regions, and its expression in Escherichia coli."
    Oh S.-J., Kim Y.-C., Park Y.-W., Min S.-Y., Kim I.-S., Kang H.-S.
    Gene 56:87-97(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "A common precursor for the two subunits of the penicillin acylase from Escherichia coli ATCC11105."
    Oliver G., Valle F., Rosetti F., Gomez-Pedrozo M., Santamaria P., Gosset G., Bolivar F.
    Gene 40:9-14(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-368.
    Strain: W / ATCC 11105 / DSM 1900.
  4. "Characterization of the regulatory region of the Escherichia coli penicillin acylase structural gene."
    Valle F., Gosset G., Tenorio B., Oliver G., Bolivar F.
    Gene 50:119-122(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-368.
  5. "Structure of the penicillin acylase gene from Escherichia coli: a periplasmic enzyme that undergoes multiple proteolytic processing."
    Bruns W., Hoppe J., Tsai H., Bruning H.J., Maywald F., Collins J., Mayer H.
    J. Mol. Appl. Genet. 3:36-44(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-350 AND 741-846.
  6. "Transcriptional and gene fusion analyses of the Escherichia coli penicillin amidase gene expression."
    Radoja S., Francetic O., Stojicevic N., Moric I., Glisin S., Konstantinovic M.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
    Strain: W / ATCC 11105 / DSM 1900.
  7. "Site-directed chemical conversion of serine to cysteine in penicillin acylase from Escherichia coli ATCC 11105. Effect on conformation and catalytic activity."
    Slade A., Horrocks A.J., Lindsay C.D., Dunbar B., Virden R.
    Eur. J. Biochem. 197:75-80(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-36 AND 291-299.
    Strain: W / ATCC 11105 / DSM 1900.
  8. "Primary structure requirements for the maturation in vivo of penicillin acylase from Escherichia coli ATCC 11105."
    Sizmann D., Keilmann C., Boeck A.
    Eur. J. Biochem. 192:143-151(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  9. "Penicillin acylase has a single-amino-acid catalytic centre."
    Duggleby H.J., Tolley S.P., Hill C.P., Dodson E.J., Dodson G., Moody P.C.E.
    Nature 373:264-268(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MUTAGENESIS OF SER-290.
    Strain: W / ATCC 11105 / DSM 1900.
  10. "Crystal structures of penicillin acylase enzyme-substrate complexes: structural insights into the catalytic mechanism."
    McVey C.E., Walsh M.A., Dodson G.G., Wilson K.S., Brannigan J.A.
    J. Mol. Biol. 313:139-150(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 27-235.

Entry informationi

Entry nameiPAC_ECOLX
AccessioniPrimary (citable) accession number: P06875
Secondary accession number(s): Q47434
, Q47435, Q47436, Q47437, Q60253
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 1, 1989
Last modified: May 11, 2016
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.