P05364 (AMPC_ENTCL) 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

Organism

Enterobacter cloacae

Taxonomic identifier

550 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Enterobacter › Enterobacter cloacae complex

Protein attributes

Sequence length	381 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.
Subcellular location	Periplasm By similarity.
Miscellaneous	The sequence shown is that of strain P99.
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
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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Chain

21 – 381

361

Beta-lactamase

PRO_0000016959

Regions

Region

335 – 337

3

Substrate binding

Sites

Active site

84

1

Acyl-ester intermediate

Active site

170

1

Proton acceptor

Natural variations

Natural variant

3

1

R → I in strain: MHN1.

Natural variant

14

1

I → L in strain: MHN1.

Natural variant

21

1

T → A in strain: MHN1.

Natural variant

36

1

I → V in strain: MHN1 and Q980R.

Natural variant

58

1

P → S in strain: MHN1.

Natural variant

108

1

A → P in strain: MHN1 and Q980R.

Natural variant

152

1

L → V in strain: Q980R.

Natural variant

262

1

N → K in strain: MHN1.

Natural variant

319

1

A → V in strain: Q980R.

Natural variant

362

1

T → K in strain: MHN1.

Secondary structure

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381

Helix Strand Turn

Details...

Helix

25 – 42

18

Beta strand

46 – 54

9

Beta strand

57 – 67

11

Turn

68 – 71

4

Beta strand

79 – 81

3

Helix

83 – 85

3

Helix

86 – 99

14

Helix

109 – 112

4

Helix

119 – 121

3

Helix

126 – 130

5

Helix

148 – 157

10

Beta strand

166 – 168

3

Helix

172 – 182

11

Helix

184 – 186

3

Helix

190 – 197

8

Turn

198 – 203

6

Beta strand

207 – 210

4

Helix

213 – 218

6

Beta strand

222 – 224

3

Beta strand

227 – 229

3

Helix

237 – 241

5

Helix

247 – 258

12

Helix

260 – 262

3

Helix

266 – 275

10

Beta strand

277 – 282

6

Beta strand

285 – 287

3

Beta strand

292 – 297

6

Helix

300 – 307

8

Helix

309 – 312

4

Beta strand

319 – 325

7

Beta strand

329 – 338

10

Beta strand

343 – 349

7

Helix

350 – 352

3

Beta strand

354 – 362

9

Helix

366 – 379

14

Sequences

	Sequence		Length	Mass (Da)
	P05364 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 90F56ABAF07AA304	FASTA	381	41,302
	10 20 30 40 50 60 MMRKSLCCAL LLGISCSALA TPVSEKQLAE VVANTITPLM KAQSVPGMAV AVIYQGKPHY 70 80 90 100 110 120 YTFGKADIAA NKPVTPQTLF ELGSISKTFT GVLGGDAIAR GEISLDDAVT RYWPQLTGKQ 130 140 150 160 170 180 WQGIRMLDLA TYTAGGLPLQ VPDEVTDNAS LLRFYQNWQP QWKPGTTRLY ANASIGLFGA 190 200 210 220 230 240 LAVKPSGMPY EQAMTTRVLK PLKLDHTWIN VPKAEEAHYA WGYRDGKAVR VSPGMLDAQA 250 260 270 280 290 300 YGVKTNVQDM ANWVMANMAP ENVADASLKQ GIALAQSRYW RIGSMYQGLG WEMLNWPVEA 310 320 330 340 350 360 NTVVEGSDSK VALAPLPVAE VNPPAPPVKA SWVHKTGSTG GFGSYVAFIP EKQIGIVMLA 370 380 NTSYPNPARV EAAYHILEAL Q

References

[1]	"Sequence and comparative analysis of three Enterobacter cloacae ampC beta-lactamase genes and their products." Galleni M., Lindberg F., Normark S., Cole S., Honore N., Joris B., Frere J.-M. Biochem. J. 250:753-760(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MHN1, P99 and Q908R.
[2]	"Evolution of an enzyme activity: crystallographic structure at 2-A resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase." Lobkovsky E., Moews P.C., Liu H., Zhao H., Frere J.-M., Knox J.R. Proc. Natl. Acad. Sci. U.S.A. 90:11257-11261(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). Strain: P99.
[3]	"Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a beta-lactamase transition-state analog." Lobkovsky E., Billings E.M., Moews P.C., Rahil J., Pratt R.F., Knox J.R. Biochemistry 33:6762-6772(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). Strain: P99.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X07274 Genomic DNA. Translation: CAA30257.1.
X08082 Genomic DNA. Translation: CAA30879.1.
X08081 Genomic DNA. Translation: CAA30878.1.

PIR

PNKBP. S00404.
PNKBQ. S00405.
PNKBM. S00406.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BLS	X-ray	2.30	A/B	21-381	[»]
1GCE	X-ray	1.80	A	21-381	[»]
1RGZ	X-ray	1.37	A	22-381	[»]
1XX2	X-ray	1.88	A/B	21-381	[»]
1Y54	X-ray	2.10	A	21-381	[»]
2Q9M	X-ray	2.05	A	22-380	[»]
2Q9N	X-ray	2.20	A	22-380	[»]
3S4X	X-ray	1.95	A	21-381	[»]

ProteinModelPortal

P05364.

SMR

P05364. Positions 22-380.

ModBase

Search...

Protein family/group databases

MEROPS

S12.006.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P05364.

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

P05364.

ChEMBL

CHEMBL2725.

EvolutionaryTrace

P05364.

Entry information

Entry name

AMPC_ENTCL

Accession

Primary (citable) accession number: P05364

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	April 3, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program