Q56415 (FOSA_SERMA) 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
Synonyms:	fos

Organism

Serratia marcescens

Taxonomic identifier

615 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	141 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. Ref.2
Subcellular location	Cytoplasm Ref.1.
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
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 – 141

141

Glutathione transferase FosA

PRO_0000164044

Sites

Metal binding

7

1

Manganese

Metal binding

67

1

Manganese

Metal binding

113

1

Manganese

Experimental info

Mutagenesis

7

1

H → A: Strong decrease in fosfomycin resistance. Ref.3

Mutagenesis

7

1

H → Q: Decrease in fosfomycin resistance. Ref.3

Mutagenesis

67

1

H → A: Loss of fosfomycin resistance. Ref.3

Mutagenesis

67

1

H → Q: Decrease in fosfomycin resistance. Ref.3

Mutagenesis

113

1

E → A: Strong decrease in fosfomycin resistance. Ref.3

Mutagenesis

113

1

E → Q: Decrease in fosfomycin resistance. Ref.3

Secondary structure

1

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141

Helix Strand Turn

Details...

Beta strand

4 – 13

10

Helix

15 – 23

9

Beta strand

29 – 34

6

Beta strand

37 – 42

6

Beta strand

45 – 51

7

Helix

60 – 62

3

Beta strand

67 – 71

5

Turn

74 – 76

3

Helix

77 – 86

10

Beta strand

91 – 93

3

Beta strand

97 – 105

9

Beta strand

111 – 116

6

Helix

119 – 128

10

Beta strand

135 – 137

3

Sequences

	Sequence		Length	Mass (Da)
	Q56415 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7BA4E5BF33FF3315	FASTA	141	15,959
	10 20 30 40 50 60 MLQSLNHLTL AVSDLQKSVT FWHELLGLTL HARWNTGAYL TCGDLWVCLS YDEARQYVPP 70 80 90 100 110 120 QESDYTHYAF TVAEEDFEPL SQRLEQAGVT IWKQNKSEGA SFYFLDPDGH KLELHVGSLA 130 140 ARLAACREKP YAGMVFTSDE A

References

[1]	"Nucleotide sequence and intracellular location of the product of the fosfomycin resistance gene from transposon Tn2921." Navas J., Leon J., Arroyo M., Garcia Lobo J.M. Antimicrob. Agents Chemother. 34:2016-2018(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION. Transposon: Tn2921.
[2]	"Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases." Bernat B.A., Laughlin L.T., Armstrong R.N. Biochemistry 36:3050-3055(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, SUBUNIT.
[3]	"Elucidation of a monovalent cation dependence and characterization of the divalent cation binding site of the fosfomycin resistance protein (FosA)." Bernat B.A., Laughlin L.T., Armstrong R.N. Biochemistry 38:7462-7469(1999) [PubMed] [Europe PMC] [Abstract] Cited for: METAL-BINDING SITES, MUTAGENESIS OF HIS-7; HIS-67 AND GLU-113.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M85195 Genomic DNA. Translation: AAA98399.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NPB	X-ray	2.50	A/B/C/D/E/F	1-141	[»]

ProteinModelPortal

Q56415.

SMR

Q56415. Positions 1-140.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

Q56415.

Family and domain databases

InterPro

IPR004360. Glyas_Fos-R_dOase_dom.
[Graphical view]

Pfam

PF00903. Glyoxalase. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q56415.

Entry information

Entry name

FOSA_SERMA

Accession

Primary (citable) accession number: Q56415

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program