Beta-lactamase precursor - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P00811 (AMPC_ECOLI)

Last modified November 3, 2009. Version 104. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Beta-lactamase
    EC=3.5.2.6
Alternative name(s):
    Cephalosporinase

Gene names

Name:	ampC
Synonyms:	ampA
Ordered Locus Names:	b4150, JW4111

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Biological process	Antibiotic resistance
Cellular component	Periplasm
Domain	Signal
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	antibiotic catabolic process Inferred from electronic annotation. Source: InterPro response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro
Molecular function	beta-lactamase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
dnaK	P0A6Y8	1	EBI-1134803,EBI-542092

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Ref.1

Chain

20 – 377

358

Beta-lactamase

PRO_0000016958

Regions

Region

331 – 333

Substrate binding By similarity

Sites

Active site

Acyl-ester intermediate Ref.1

Active site

166

Proton acceptor

Experimental info

Mutagenesis

S → D, E or G: Loss of activity. Ref.9

Mutagenesis

K → Q or T: Lowers activity more than 1000-fold and increases protein stability. Ref.9

Mutagenesis

166

Y → E: Lowers activity more than 1000-fold. Ref.9

Mutagenesis

168

N → D or H: Lowers activity more than 1000-fold. Ref.9

Mutagenesis

331

K → A: Lowers activity more than 1000-fold. Ref.9

Secondary structure

377

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P00811-1 [UniParc].

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

377

41,556

        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

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References

	« Hide 'large scale' referencesShow '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: 6795623] [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: 7610040] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 7041115] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
[6]	"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: 9819201] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[7]	"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: 10595535] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[8]	"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: 11478888] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGUE.
[9]	"Structural bases of stability-function tradeoffs in enzymes." Beadle B.M., Shoichet B.K. J. Mol. Biol. 321:285-296(2002) [PubMed: 12144785] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS), MUTAGENESIS OF SER-80; LYS-83; TYR-166; ASN-168 AND LYS-331.
[10]	"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: 12526668] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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.

PIR

QKEC. A01007.

RefSeq

AP_004653.1.
NP_418574.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C3B	X-ray	2.25	A/B	20-377	[»]
1FCM	X-ray	2.46	A/B	20-377	[»]
1FCN	X-ray	2.35	A/B	20-377	[»]
1FCO	X-ray	2.20	A/B	20-377	[»]
1FSW	X-ray	1.90	A/B	20-376	[»]
1FSY	X-ray	1.75	A/B	20-376	[»]
1GA9	X-ray	2.10	A/B	20-377	[»]
1I5Q	X-ray	1.83	A/B	20-377	[»]
1IEL	X-ray	2.00	A/B	20-377	[»]
1IEM	X-ray	2.30	A/B	20-377	[»]
1KDS	X-ray	2.15	A/B	20-377	[»]
1KDW	X-ray	2.28	A/B	20-377	[»]
1KE0	X-ray	2.30	A/B	20-377	[»]
1KE3	X-ray	2.15	A/B	20-377	[»]
1KE4	X-ray	1.72	A/B	20-377	[»]
1KVL	X-ray	1.53	A/B	20-377	[»]
1KVM	X-ray	2.06	A/B	20-377	[»]
1L0D	X-ray	1.53	A/B	20-377	[»]
1L0E	X-ray	1.90	A/B	20-377	[»]
1L0F	X-ray	1.66	A/B	20-377	[»]
1L0G	X-ray	1.50	A/B	20-377	[»]
1L2S	X-ray	1.94	A/B	20-377	[»]
1LL5	X-ray	1.80	A/B	20-377	[»]
1LL9	X-ray	1.87	A/B	20-377	[»]
1LLB	X-ray	1.72	A/B	20-377	[»]
1MXO	X-ray	1.83	A/B	20-377	[»]
1MY8	X-ray	1.72	A/B	20-377	[»]
1O07	X-ray	1.71	A/B	20-377	[»]
1PI4	X-ray	1.39	A/B	20-377	[»]
1PI5	X-ray	1.49	A/B	20-377	[»]
1XGI	X-ray	1.96	A/B	20-377	[»]
1XGJ	X-ray	1.97	A/B	20-377	[»]
2BLS	X-ray	2.00	A/B	20-377	[»]
2FFY	X-ray	1.07	A/B	20-377	[»]
2HDQ	X-ray	2.10	A/B	20-377	[»]
2HDR	X-ray	2.20	A/B	20-377	[»]
2HDS	X-ray	1.16	A/B	20-377	[»]
2HDU	X-ray	1.49	A/B	20-377	[»]
2I72	X-ray	2.20	A/B	20-377	[»]
2P9V	X-ray	1.80	A/B	20-377	[»]
2PU2	X-ray	1.86	A/B	20-377	[»]
2PU4	X-ray	2.00	A/B	20-377	[»]
2R9W	X-ray	1.80	A/B	20-377	[»]
2R9X	X-ray	1.90	A/B	20-377	[»]
2RCX	X-ray	2.00	A/B	20-377	[»]
3BLS	X-ray	2.30	A/B	20-377	[»]
3BM6	X-ray	2.10	A/B	20-377	[»]
3FKV	X-ray	1.85	A/B	20-377	[»]
3FKW	X-ray	1.50	A/B	20-377	[»]
3GQZ	X-ray	1.80	A/B	20-377	[»]
3GR2	X-ray	1.80	A/B	20-377	[»]
3GRJ	X-ray	2.49	A/B	20-377	[»]
3GSG	X-ray	2.10	A/B	20-377	[»]
3GTC	X-ray	1.90	A/B	20-377	[»]
3GV9	X-ray	1.80	A/B	20-377	[»]
3GVB	X-ray	1.80	A/B	20-377	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P00811. 1 interaction.

STRING

P00811.

PTM databases

PhosSite

P00811.

2-D gel databases

SWISS-2DPAGE

P00811.

ECO2DBASE

I035.7. 6TH EDITION.

Genome annotation databases

GeneID

948669.

GenomeReviews

Gene locus JW4111 in contig AP009048_GR.
Gene locus b4150 in contig U00096_GR.

KEGG

ecj:JW4111.
eco:b4150.

Organism-specific databases

EchoBASE

EB0038.

EcoGene

EG10040. ampC.

CMR

Search...

Phylogenomic databases

HOGENOM

P00811.

OMA

AGRFVWK.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10040-MON.
MetaCyc:EG10040-MON.

Gene expression databases

Genevestigator

P00811.

Family and domain databases

InterPro

IPR001586. Beta_lactam_C_AS.
IPR001466. Beta_lactamase-related.
[Graphical view]

Pfam

PF00144. Beta-lactamase. 1 hit.
[Graphical view]

PROSITE

PS00336. BETA_LACTAMASE_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00456. Cefalotin.
DB01147. Cloxacillin.

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Entry information

Entry name

AMPC_ECOLI

Accession

Primary (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:	November 3, 2009
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents