P13661 (BLO1_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-lactamase OXA-1
EC=3.5.2.6

Alternative name(s):
Penicillinase

Gene names

Name:	bla
Synonyms:	oxa1

Encoded on

Plasmid RGN238

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	276 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 is an oxacillin-hydrolyzing beta-lactamase.
Catalytic activity	A beta-lactam + H2O = a substituted beta-amino acid.
Subunit structure	Monomer. Ref.3
Sequence similarities	Belongs to the class-D beta-lactamase family.

Ontologies

Keywords
Biological process	Antibiotic resistance
Domain	Signal
Molecular function	Hydrolase
Technical term	3D-structure Direct protein sequencing Plasmid Transposable element
Gene Ontology (GO)
Biological_process	antibiotic catabolic process Inferred from electronic annotation. Source: InterPro peptidoglycan-based cell wall biogenesis Inferred from electronic annotation. Source: InterPro response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	beta-lactamase activity Inferred from electronic annotation. Source: EC penicillin binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Ref.3

Chain

26 – 276

251

Beta-lactamase OXA-1

PRO_0000017024

Regions

Region

238 – 240

3

Substrate binding By similarity

Sites

Active site

71

1

Acyl-ester intermediate

Amino acid modifications

Modified residue

74

1

N6-carboxylysine

Secondary structure

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276

Helix Strand Turn

Details...

Helix

30 – 36

7

Turn

37 – 39

3

Beta strand

40 – 48

9

Turn

49 – 51

3

Beta strand

54 – 58

5

Helix

60 – 63

4

Helix

70 – 72

3

Helix

73 – 83

11

Helix

103 – 105

3

Helix

111 – 116

6

Helix

120 – 130

11

Helix

132 – 141

10

Helix

158 – 161

4

Beta strand

164 – 167

4

Helix

172 – 183

12

Beta strand

187 – 189

3

Helix

191 – 200

10

Beta strand

202 – 205

4

Beta strand

211 – 220

10

Beta strand

227 – 236

10

Beta strand

242 – 251

10

Helix

259 – 274

16

Sequences

	Sequence		Length	Mass (Da)
	P13661 [UniParc]. Last modified February 10, 2009. Version 2. Checksum: 5ADF7626422BA124	FASTA	276	30,880
	10 20 30 40 50 60 MKNTIHINFA IFLIIANIIY SSASASTDIS TVASPLFEGT EGCFLLYDAS TNAEIAQFNK 70 80 90 100 110 120 AKCATQMAPD STFKIALSLM AFDAEIIDQK TIFKWDKTPK GMEIWNSNHT PKTWMQFSVV 130 140 150 160 170 180 WVSQEITQKI GLNKIKNYLK DFDYGNQDFS GDKERNNGLT EAWLESSLKI SPEEQIQFLR 190 200 210 220 230 240 KIINHNLPVK NSAIENTIEN MYLQDLDNST KLYGKTGAGF TANRTLQNGW FEGFIISKSG 250 260 270 HKYVFVSALT GNLGSNLTSS IKAKKNAITI LNTLNL

References

[1]	"Precise insertion of antibiotic resistance determinants into Tn21-like transposons: nucleotide sequence of the OXA-1 beta-lactamase gene." Ouellette M., Bissonnette L., Roy P.H. Proc. Natl. Acad. Sci. U.S.A. 84:7378-7382(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Transposon: Tn2603.
[2]	Ouellette M., Roy P.H. Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 131.
[3]	"Comparison of beta-lactamases of classes A and D: 1.5-A crystallographic structure of the class D OXA-1 oxacillinase." Sun T., Nukaga M., Mayama K., Braswell E.H., Knox J.R. Protein Sci. 12:82-91(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 26-276, PROTEIN SEQUENCE OF N-TERMINUS, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J02967 Genomic DNA. Translation: AAA91586.2.

PIR

A39880.

RefSeq

NP_957554.1. NC_005327.1.
YP_006953880.1. NC_019089.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M6K	X-ray	1.50	A/B	26-276	[»]
3ISG	X-ray	1.40	A/B	26-276	[»]

ProteinModelPortal

P13661.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

13906817.
2716479.

Phylogenomic databases

ProtClustDB

CLSK763259.

Enzyme and pathway databases

SABIO-RK

P13661.

Family and domain databases

Gene3D

3.40.710.10. 1 hit.

InterPro

IPR012338. Beta-lactam/transpept-like.
IPR002137. Beta-lactam_class-D_AS.
IPR001460. PCN-bd_Tpept.
[Graphical view]

Pfam

PF00905. Transpeptidase. 1 hit.
[Graphical view]

SUPFAM

SSF56601. PBP_transp_fold. 1 hit.

PROSITE

PS00337. BETA_LACTAMASE_D. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL4951.

EvolutionaryTrace

P13661.

Entry information

Entry name

BLO1_ECOLX

Accession

Primary (citable) accession number: P13661

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	February 10, 2009
Last modified:	April 3, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program