Q9I4K6 (FOSA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione transferase FosA
EC=2.5.1.18

Alternative name(s):
Fosfomycin resistance protein

Gene names

Name:	fosA
Ordered Locus Names:	PA1129

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas aeruginosa group › Pseudomonas aeruginosa

Protein attributes

Sequence length	135 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin. Ref.2
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Cofactor	Manganese. Ref.2
Enzyme regulation	Requires the monovalent cation K+ for optimal activity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the fosfomycin resistance protein family.

Ontologies

Keywords
Biological process	Antibiotic resistance
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding Potassium
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glutathione transferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 135

135

Glutathione transferase FosA

PRO_0000164043

Sites

Metal binding

7

1

Manganese

Metal binding

64

1

Manganese

Metal binding

110

1

Manganese

Secondary structure

1

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135

Helix Strand Turn

Details...

Beta strand

2 – 13

12

Helix

15 – 24

10

Beta strand

29 – 34

6

Beta strand

37 – 42

6

Beta strand

45 – 51

7

Beta strand

60 – 62

3

Beta strand

64 – 69

6

Helix

71 – 73

3

Helix

74 – 83

10

Beta strand

88 – 90

3

Beta strand

94 – 96

3

Beta strand

98 – 102

5

Beta strand

108 – 113

6

Helix

116 – 125

10

Sequences

	Sequence		Length	Mass (Da)
	Q9I4K6 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 0D75F174291A2366	FASTA	135	15,124
	10 20 30 40 50 60 MLTGLNHLTL AVADLPASIA FYRDLLGFRL EARWDQGAYL ELGSLWLCLS REPQYGGPAA 70 80 90 100 110 120 DYTHYAFGIA AADFARFAAQ LRAHGVREWK QNRSEGDSFY FLDPDGHRLE AHVGDLRSRL 130 AACRQAPYAG MRFAD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V. Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]	"Crystal structure of a genomically encoded fosfomycin resistance protein (FosA) at 1.19 A resolution by MAD phasing off the L-III edge of Tl(+)." Rife C.L., Pharris R.E., Newcomer M.E., Armstrong R.N. J. Am. Chem. Soc. 124:11001-11003(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.19 ANGSTROMS) IN COMPLEX WITH FOSFOMYCIN, FUNCTION, COFACTOR. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE004091 Genomic DNA. Translation: AAG04518.1.

PIR

E83503.

RefSeq

NP_249820.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LQK	X-ray	1.35	A/B	1-135	[»]
1LQO	X-ray	2.00	A/B	1-135	[»]
1LQP	X-ray	1.19	A/B	1-135	[»]
1NKI	X-ray	0.95	A/B	1-135	[»]
1NNR	X-ray	2.25	A/B	1-135	[»]

ProteinModelPortal

Q9I4K6.

SMR

Q9I4K6. Positions 1-134.

ModBase

Search...

Protein-protein interaction databases

STRING

208964.PA1129.

Protocols and materials databases

DNASU

877785.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

877785.

KEGG

pae:PA1129.

PATRIC

19836576. VBIPseAer58763_1174.

Organism-specific databases

PseudoCAP

PA1129.

Phylogenomic databases

eggNOG

COG0346.

HOGENOM

HOG000232023.

OMA

ALNEETH.

ProtClustDB

CLSK2747893.

Family and domain databases

InterPro

IPR025870. Glyoxalase-like_dom.
[Graphical view]

Pfam

PF12681. Glyoxalase_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9I4K6.

Entry information

Entry name

FOSA_PSEAE

Accession

Primary (citable) accession number: Q9I4K6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program