P14489 (BLO10_PSEAI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-lactamase OXA-10
EC=3.5.2.6

Alternative name(s):
Beta-lactamase PSE-2

Gene names

Name:	bla
Synonyms:	oxa10, pse2

Encoded on

Plasmid pMON234

Organism

Pseudomonas aeruginosa

Taxonomic identifier

287 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	266 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	Hydrolyzes both carbenicillin and oxacillin.
Catalytic activity	A beta-lactam + H2O = a substituted beta-amino acid.
Sequence similarities	Belongs to the class-D beta-lactamase family.

Ontologies

Keywords
Biological process	Antibiotic resistance
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	3D-structure 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 – 20

20

Chain

21 – 266

246

Beta-lactamase OXA-10

PRO_0000017030

Regions

Region

205 – 207

3

Substrate binding By similarity

Sites

Active site

67

1

Acyl-ester intermediate

Amino acid modifications

Modified residue

70

1

N6-carboxylysine

Disulfide bond

44 ↔ 51

Secondary structure

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266

Helix Strand Turn

Details...

Helix

26 – 28

3

Helix

29 – 34

6

Beta strand

39 – 47

9

Beta strand

50 – 54

5

Helix

56 – 59

4

Helix

66 – 69

4

Helix

70 – 79

10

Helix

100 – 102

3

Helix

108 – 113

6

Helix

117 – 127

11

Helix

129 – 138

10

Turn

150 – 155

6

Beta strand

156 – 158

3

Helix

163 – 174

12

Beta strand

178 – 180

3

Helix

182 – 191

10

Beta strand

193 – 197

5

Beta strand

200 – 208

9

Beta strand

214 – 216

3

Beta strand

218 – 228

11

Beta strand

231 – 242

12

Helix

244 – 248

5

Helix

249 – 260

12

Sequences

	Sequence		Length	Mass (Da)
	P14489 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 9ABFF429D028F240	FASTA	266	29,507
	10 20 30 40 50 60 MKTFAAYVII ACLSSTALAG SITENTSWNK EFSAEAVNGV FVLCKSSSKS CATNDLARAS 70 80 90 100 110 120 KEYLPASTFK IPNAIIGLET GVIKNEHQVF KWDGKPRAMK QWERDLTLRG AIQVSAVPVF 130 140 150 160 170 180 QQIAREVGEV RMQKYLKKFS YGNQNISGGI DKFWLEGQLR ISAVNQVEFL ESLYLNKLSA 190 200 210 220 230 240 SKENQLIVKE ALVTEAAPEY LVHSKTGFSG VGTESNPGVA WWVGWVEKET EVYFFAFNMD 250 260 IDNESKLPLR KSIPTKIMES EGIIGG

References

[1]	"Sequence of PSE-2 beta-lactamase." Huovinen P., Huovinen S., Jacoby G.A. Antimicrob. Agents Chemother. 32:134-136(1988) [PubMed: 3126705] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Transposon: Tn1404.
[2]	"Insights into class D beta-lactamases are revealed by the crystal structure of the OXA10 enzyme from Pseudomonas aeruginosa." Maveyraud L., Golemi D., Kotra L.P., Tranier S., Vakulenko S., Mobashery S., Samama J.-P. Structure 8:1289-1298(2000) [PubMed: 11188693] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 21-266, CARBAMYLATION AT LYS-70.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U37105 Genomic DNA. Translation: AAB60534.1.
J03427 Genomic DNA. Translation: AAA25648.1.

PIR

S06462.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E3U	X-ray	1.66	A/B/C/D	21-266	[»]
1E4D	X-ray	1.80	A/B/C/D	21-266	[»]
1EWZ	X-ray	2.40	A/B/C/D	21-266	[»]
1FOF	X-ray	2.00	A/B	20-265	[»]
1K4E	X-ray	2.00	A/B	20-266	[»]
1K4F	X-ray	1.60	A/B	20-266	[»]
1K54	X-ray	1.70	A/B/C/D	21-266	[»]
1K55	X-ray	1.39	A/B/C/D	21-266	[»]
1K56	X-ray	1.70	A/B/C/D	21-266	[»]
1K57	X-ray	1.90	A/B/C/D	21-266	[»]
1K6R	X-ray	2.30	A/B	20-266	[»]
1K6S	X-ray	2.03	A/B	20-266	[»]
2HP5	X-ray	2.70	A/B/C/D	20-266	[»]
2HP6	X-ray	2.20	A/B	20-266	[»]
2HP9	X-ray	2.50	A/B	20-266	[»]
2HPB	X-ray	2.05	A/B	20-266	[»]
2RL3	X-ray	1.90	A/B	20-266	[»]
2WGI	X-ray	2.85	A/B	20-266	[»]
2WGV	X-ray	1.80	A/B	20-266	[»]
2WGW	X-ray	1.80	A/B	20-266	[»]
2WKH	X-ray	1.79	A/B	20-266	[»]
2WKI	X-ray	2.10	A/B	20-266	[»]
2X01	X-ray	1.90	A/B	20-266	[»]
2X02	X-ray	1.35	A/B	20-266	[»]
3LCE	X-ray	2.00	A/B/C/D	21-266	[»]

ProteinModelPortal

P14489.

SMR

P14489. Positions 21-266.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.40.710.10. G3DSA:3.40.710.10. 1 hit.

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

DrugBank

DB00760. Meropenem.

Entry information

Entry name

BLO10_PSEAI

Accession

Primary (citable) accession number: P14489

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	November 16, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program