P00811 (AMPC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

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

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 process	Antibiotic resistance
Cellular component	Periplasm
Domain	Signal
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
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 direct assay PubMed 9324260. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.1

Chain

20 – 377

358

Beta-lactamase

PRO_0000016958

Regions

Region

331 – 333

3

Substrate binding By similarity

Sites

Active site

80

1

Acyl-ester intermediate Ref.1

Active site

166

1

Proton acceptor

Experimental info

Mutagenesis

80

1

S → D, E or G: Loss of activity. Ref.10

Mutagenesis

83

1

K → Q or T: Lowers activity more than 1000-fold and increases protein stability. Ref.10

Mutagenesis

166

1

Y → E: Lowers activity more than 1000-fold. Ref.10

Mutagenesis

168

1

N → D or H: Lowers activity more than 1000-fold. Ref.10

Mutagenesis

331

1

K → A: Lowers activity more than 1000-fold. Ref.10

Secondary structure

1

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377

Helix Strand Turn

Details...

Helix

22 – 39

18

Beta strand

42 – 50

9

Beta strand

53 – 63

11

Turn

64 – 67

4

Beta strand

75 – 77

3

Helix

79 – 81

3

Helix

82 – 95

14

Helix

105 – 108

4

Helix

115 – 117

3

Helix

122 – 126

5

Helix

144 – 153

10

Beta strand

162 – 164

3

Helix

168 – 178

11

Turn

179 – 183

5

Helix

186 – 193

8

Turn

194 – 199

6

Beta strand

204 – 206

3

Helix

209 – 214

6

Beta strand

218 – 220

3

Beta strand

223 – 225

3

Turn

229 – 231

3

Helix

233 – 236

4

Beta strand

240 – 242

3

Helix

243 – 254

12

Helix

256 – 258

3

Helix

262 – 271

10

Beta strand

273 – 278

6

Beta strand

281 – 283

3

Beta strand

288 – 293

6

Helix

296 – 301

6

Beta strand

303 – 305

3

Beta strand

306 – 308

3

Beta strand

310 – 313

4

Beta strand

315 – 321

7

Beta strand

325 – 335

11

Beta strand

338 – 345

8

Helix

346 – 348

3

Beta strand

350 – 358

9

Helix

362 – 376

15

Sequences

	Sequence		Length	Mass (Da)
	P00811 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 3C6FB4FE4EF96C9F	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

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] [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 277:1453-1474(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.

PIR

QKEC. A01007.

RefSeq

NP_418574.1. NC_000913.2.
YP_492295.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3IWI	X-ray	1.64	A/B	20-377	[»]
3IWO	X-ray	1.90	A/B	20-377	[»]
3IWQ	X-ray	1.84	A/B	20-377	[»]
3IXB	X-ray	1.63	A/B	20-377	[»]
3IXD	X-ray	2.64	A/B	20-377	[»]
3IXG	X-ray	2.14	A/B	20-377	[»]
3IXH	X-ray	2.30	A/B	20-377	[»]
3O86	X-ray	1.60	A/B	20-377	[»]
3O87	X-ray	1.78	A/B	20-377	[»]
3O88	X-ray	1.64	A/B	20-377	[»]
4E3I	X-ray	1.60	A/B	20-377	[»]
4E3J	X-ray	1.80	A/B	20-377	[»]
4E3K	X-ray	1.43	A/B	20-377	[»]
4E3L	X-ray	1.43	A/B	20-377	[»]
4E3M	X-ray	1.44	A/B	20-377	[»]
4E3N	X-ray	1.49	A/B	20-377	[»]
4E3O	X-ray	1.60	A/B	20-377	[»]

ProteinModelPortal

P00811.

SMR

P00811. Positions 20-377.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00811. 1 interaction.

STRING

511145.b4150.

Protein family/group databases

MEROPS

S12.006.

PTM databases

PhosSite

P0809371.

2D gel databases

SWISS-2DPAGE

P00811.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77110; AAC77110; b4150.
BAE78154; BAE78154; BAE78154.

GeneID

12932283.
948669.

KEGG

ecj:Y75_p4039.
eco:b4150.

PATRIC

32123873. VBIEscCol129921_4284.

Organism-specific databases

EchoBASE

EB0038.

EcoGene

EG10040. ampC.

Phylogenomic databases

eggNOG

COG1680.

HOGENOM

HOG000267102.

KO

K01467.

OMA

TSIYAGN.

ProtClustDB

PRK11289.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10040-MONOMER.
ECOL316407:JW4111-MONOMER.
MetaCyc:EG10040-MONOMER.

SABIO-RK

P00811.

Gene expression databases

Genevestigator

P00811.

Family and domain databases

Gene3D

3.40.710.10. 1 hit.

InterPro

IPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR001586. Beta-lactam_class-C_AS.
[Graphical view]

Pfam

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

SUPFAM

SSF56601. PBP_transp_fold. 1 hit.

PROSITE

PS00336. BETA_LACTAMASE_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P00811.

ChEMBL

CHEMBL2026.

DrugBank

DB00456. Cefalotin.
DB01147. Cloxacillin.

EvolutionaryTrace

P00811.

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:	May 1, 2013
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program