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P00811 (AMPC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-lactamase

EC=3.5.2.6
Alternative name(s):
Cephalosporinase
Gene names
Name:ampC
Synonyms:ampA
Ordered Locus Names:b4150, JW4111
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.

Catalytic activity

A beta-lactam + H2O = a substituted beta-amino acid.

Subunit structure

Monomer.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the class-C beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processantibiotic catabolic process

Inferred from electronic annotation. Source: InterPro

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentouter membrane-bounded periplasmic space

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-lactamase activity

Inferred from direct assay PubMed 9324260. Source: EcoliWiki

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.1
Chain20 – 377358Beta-lactamase
PRO_0000016958

Regions

Region331 – 3333Substrate binding By similarity

Sites

Active site801Acyl-ester intermediate Ref.1
Active site1661Proton acceptor

Experimental info

Mutagenesis801S → D, E or G: Loss of activity. Ref.10
Mutagenesis831K → Q or T: Lowers activity more than 1000-fold and increases protein stability. Ref.10
Mutagenesis1661Y → E: Lowers activity more than 1000-fold. Ref.10
Mutagenesis1681N → D or H: Lowers activity more than 1000-fold. Ref.10
Mutagenesis3311K → A: Lowers activity more than 1000-fold. Ref.10

Secondary structure

........................................................................ 377
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00811 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 3C6FB4FE4EF96C9F

FASTA37741,556
        10         20         30         40         50         60 
MFKTTLCALL ITASCSTFAA PQQINDIVHR TITPLIEQQK IPGMAVAVIY QGKPYYFTWG 

        70         80         90        100        110        120 
YADIAKKQPV TQQTLFELGS VSKTFTGVLG GDAIARGEIK LSDPTTKYWP ELTAKQWNGI 

       130        140        150        160        170        180 
TLLHLATYTA GGLPLQVPDE VKSSSDLLRF YQNWQPAWAP GTQRLYANSS IGLFGALAVK 

       190        200        210        220        230        240 
PSGLSFEQAM QTRVFQPLKL NHTWINVPPA EEKNYAWGYR EGKAVHVSPG ALDAEAYGVK 

       250        260        270        280        290        300 
STIEDMARWV QSNLKPLDIN EKTLQQGIQL AQSRYWQTGD MYQGLGWEML DWPVNPDSII 

       310        320        330        340        350        360 
NGSDNKIALA ARPVKAITPP TPAVRASWVH KTGATGGFGS YVAFIPEKEL GIVMLANKNY 

       370 
PNPARVDAAW QILNALQ 

« Hide

References

« Hide 'large scale' references
[1]"ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type."
Jaurin B., Grundstroem T.
Proc. Natl. Acad. Sci. U.S.A. 78:4897-4901(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-31.
Strain: K12.
[2]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Overlap between ampC and frd operons on the Escherichia coli chromosome."
Grundstroem T., Jaurin B.
Proc. Natl. Acad. Sci. U.S.A. 79:1111-1115(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
[6]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[7]"Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design."
Usher K.C., Blaszczak L.C., Weston G.S., Shoichet B.K., Remington S.J.
Biochemistry 37:16082-16092(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[8]"The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase."
Powers R.A., Blazquez J., Weston G.S., Morosini M.I., Baquero F., Shoichet B.K.
Protein Sci. 8:2330-2337(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[9]"Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-lactamase: implications for resistance mutations and inhibitor design."
Powers R.A., Caselli E., Focia P.J., Prati F., Shoichet B.K.
Biochemistry 40:9207-9214(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGUE.
[10]"Structural bases of stability-function tradeoffs in enzymes."
Beadle B.M., Shoichet B.K.
J. Mol. Biol. 321:285-296(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS), MUTAGENESIS OF SER-80; LYS-83; TYR-166; ASN-168 AND LYS-331.
[11]"Nanomolar inhibitors of AmpC beta-lactamase."
Morandi F., Caselli E., Morandi S., Focia P.J., Blazquez J., Shoichet B.K., Prati F.
J. Am. Chem. Soc. 125:685-695(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01611 Genomic DNA. Translation: AAA23441.1.
U14003 Genomic DNA. Translation: AAA97049.1.
U00096 Genomic DNA. Translation: AAC77110.1.
AP009048 Genomic DNA. Translation: BAE78154.1.
V00277 Genomic DNA. Translation: CAA23537.1.
PIRQKEC. A01007.
RefSeqNP_418574.1. NC_000913.3.
YP_492295.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3BX-ray2.25A/B20-377[»]
1FCMX-ray2.46A/B20-377[»]
1FCNX-ray2.35A/B20-377[»]
1FCOX-ray2.20A/B20-377[»]
1FSWX-ray1.90A/B20-376[»]
1FSYX-ray1.75A/B20-376[»]
1GA9X-ray2.10A/B20-377[»]
1I5QX-ray1.83A/B20-377[»]
1IELX-ray2.00A/B20-377[»]
1IEMX-ray2.30A/B20-377[»]
1KDSX-ray2.15A/B20-377[»]
1KDWX-ray2.28A/B20-377[»]
1KE0X-ray2.30A/B20-377[»]
1KE3X-ray2.15A/B20-377[»]
1KE4X-ray1.72A/B20-377[»]
1KVLX-ray1.53A/B20-377[»]
1KVMX-ray2.06A/B20-377[»]
1L0DX-ray1.53A/B20-377[»]
1L0EX-ray1.90A/B20-377[»]
1L0FX-ray1.66A/B20-377[»]
1L0GX-ray1.50A/B20-377[»]
1L2SX-ray1.94A/B20-377[»]
1LL5X-ray1.80A/B20-377[»]
1LL9X-ray1.87A/B20-377[»]
1LLBX-ray1.72A/B20-377[»]
1MXOX-ray1.83A/B20-377[»]
1MY8X-ray1.72A/B20-377[»]
1O07X-ray1.71A/B20-377[»]
1PI4X-ray1.39A/B20-377[»]
1PI5X-ray1.49A/B20-377[»]
1XGIX-ray1.96A/B20-377[»]
1XGJX-ray1.97A/B20-377[»]
2BLSX-ray2.00A/B20-377[»]
2FFYX-ray1.07A/B20-377[»]
2HDQX-ray2.10A/B20-377[»]
2HDRX-ray2.20A/B20-377[»]
2HDSX-ray1.16A/B20-377[»]
2HDUX-ray1.49A/B20-377[»]
2I72X-ray2.20A/B20-377[»]
2P9VX-ray1.80A/B20-377[»]
2PU2X-ray1.86A/B20-377[»]
2PU4X-ray2.00A/B20-377[»]
2R9WX-ray1.80A/B20-377[»]
2R9XX-ray1.90A/B20-377[»]
2RCXX-ray2.00A/B20-377[»]
3BLSX-ray2.30A/B20-377[»]
3BM6X-ray2.10A/B20-377[»]
3FKVX-ray1.85A/B20-377[»]
3FKWX-ray1.50A/B20-377[»]
3GQZX-ray1.80A/B20-377[»]
3GR2X-ray1.80A/B20-377[»]
3GRJX-ray2.49A/B20-377[»]
3GSGX-ray2.10A/B20-377[»]
3GTCX-ray1.90A/B20-377[»]
3GV9X-ray1.80A/B20-377[»]
3GVBX-ray1.80A/B20-377[»]
3IWIX-ray1.64A/B20-377[»]
3IWOX-ray1.90A/B20-377[»]
3IWQX-ray1.84A/B20-377[»]
3IXBX-ray1.63A/B20-377[»]
3IXDX-ray2.64A/B20-377[»]
3IXGX-ray2.14A/B20-377[»]
3IXHX-ray2.30A/B20-377[»]
3O86X-ray1.60A/B20-377[»]
3O87X-ray1.78A/B20-377[»]
3O88X-ray1.64A/B20-377[»]
4E3IX-ray1.60A/B20-377[»]
4E3JX-ray1.80A/B20-377[»]
4E3KX-ray1.43A/B20-377[»]
4E3LX-ray1.43A/B20-377[»]
4E3MX-ray1.44A/B20-377[»]
4E3NX-ray1.49A/B20-377[»]
4E3OX-ray1.60A/B20-377[»]
4JXSX-ray1.90A/B20-377[»]
4JXVX-ray1.76A/B20-377[»]
4JXWX-ray2.30A/B20-377[»]
4KZ3X-ray1.67A/B20-377[»]
4KZ4X-ray1.42A/B20-377[»]
4KZ5X-ray1.35A/B20-377[»]
4KZ6X-ray1.68A/B20-377[»]
4KZ7X-ray1.43A/B20-377[»]
4KZ8X-ray2.28A/B20-377[»]
4KZ9X-ray1.72A/B20-377[»]
4KZAX-ray1.60A/B20-377[»]
4KZBX-ray1.37A/B20-377[»]
ProteinModelPortalP00811.
SMRP00811. Positions 20-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00811. 1 interaction.
STRING511145.b4150.

Chemistry

BindingDBP00811.
ChEMBLCHEMBL2026.
DrugBankDB00456. Cefalotin.
DB01147. Cloxacillin.

Protein family/group databases

MEROPSS12.006.

PTM databases

PhosSiteP0809371.

2D gel databases

SWISS-2DPAGEP00811.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77110; AAC77110; b4150.
BAE78154; BAE78154; BAE78154.
GeneID12932283.
948669.
KEGGecj:Y75_p4039.
eco:b4150.
PATRIC32123873. VBIEscCol129921_4284.

Organism-specific databases

EchoBASEEB0038.
EcoGeneEG10040. ampC.

Phylogenomic databases

eggNOGCOG1680.
HOGENOMHOG000267102.
KOK01467.
OMAKVGDMTQ.
OrthoDBEOG60SCH1.
PhylomeDBP00811.

Enzyme and pathway databases

BioCycEcoCyc:EG10040-MONOMER.
ECOL316407:JW4111-MONOMER.
MetaCyc:EG10040-MONOMER.
SABIO-RKP00811.

Gene expression databases

GenevestigatorP00811.

Family and domain databases

Gene3D3.40.710.10. 1 hit.
InterProIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR001586. Beta-lactam_class-C_AS.
[Graphical view]
PfamPF00144. Beta-lactamase. 1 hit.
[Graphical view]
SUPFAMSSF56601. SSF56601. 1 hit.
PROSITEPS00336. BETA_LACTAMASE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00811.
PROP00811.

Entry information

Entry nameAMPC_ECOLI
AccessionPrimary (citable) accession number: P00811
Secondary accession number(s): Q2M6F2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene