Q81W73 (FOSB2_BACAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Metallothiol transferase FosB 2
EC=2.5.1.-

Alternative name(s):
Fosfomycin resistance protein 2

Gene names

Name:	fosB2
Synonyms:	fosB-2
Ordered Locus Names:	BA_4109, GBAA_4109, BAS3818

Organism

Bacillus anthracis [Reference proteome] [HAMAP]

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	139 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor By similarity. HAMAP-Rule MF_01512
Cofactor	Magnesium By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the fosfomycin resistance protein family. FosB subfamily.

Ontologies

Keywords
Biological process	Antibiotic resistance
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to antibiotic Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP transferase activity, transferring alkyl or aryl (other than methyl) groups Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 139

139

Metallothiol transferase FosB 2 HAMAP-Rule MF_01512

PRO_0000164023

Sites

Metal binding

7

1

Magnesium By similarity

Metal binding

66

1

Magnesium By similarity

Metal binding

115

1

Magnesium By similarity

Secondary structure

1

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139

Helix Strand Turn

Details...

Beta strand

4 – 13

10

Helix

15 – 24

10

Beta strand

29 – 33

5

Beta strand

35 – 42

8

Beta strand

45 – 51

7

Helix

59 – 62

4

Beta strand

66 – 70

5

Helix

73 – 85

13

Helix

98 – 100

3

Beta strand

103 – 107

5

Beta strand

113 – 118

6

Helix

121 – 134

14

Sequences

	Sequence		Length	Mass (Da)
	Q81W73 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: E2F02F9F77690B4C	FASTA	139	16,525
	10 20 30 40 50 60 MLQGINHICF SVSNLEKSIE FYQKILQAKL LVKGRKLAYF DLNGLWIALN VEEDIPRNEI 70 80 90 100 110 120 KQSYTHMAFT VTNEALDHLK EVLIQNDVNI LPGRERDERD QRSLYFTDPD GHKFEFHTGT 130 LQNRLEYYKE DKKHMTFYI

References

[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'." Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A. J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE016879 Genomic DNA. Translation: AAP27834.1.
AE017334 Genomic DNA. Translation: AAT33228.1.
AE017225 Genomic DNA. Translation: AAT56119.1.

RefSeq

NP_846348.1. NC_003997.3.
YP_020753.1. NC_007530.2.
YP_030068.1. NC_005945.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4IR0	X-ray	1.60	A/B	1-139	[»]

ProteinModelPortal

Q81W73.

ModBase

Search...

Protein-protein interaction databases

STRING

198094.BA_4109.

Protocols and materials databases

DNASU

1086311.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAP27834; AAP27834; BA_4109.
AAT33228; AAT33228; GBAA_4109.
AAT56119; AAT56119; BAS3818.

GeneID

1086311.
2818084.
2851236.

KEGG

ban:BA_4109.
bar:GBAA_4109.
bat:BAS3818.

Phylogenomic databases

eggNOG

COG0346.

HOGENOM

HOG000232023.

KO

K11210.

OMA

MEDANIL.

ProtClustDB

PRK04101.

Enzyme and pathway databases

BioCyc

BANT260799:GJAJ-3875-MONOMER.
BANT261594:GJ7F-3996-MONOMER.

Family and domain databases

HAMAP

MF_01512. FosB.

InterPro

IPR025870. Glyoxalase-like_dom.
IPR022858. Metallothiol_Trafse_FosB.
[Graphical view]

Pfam

PF12681. Glyoxalase_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FOSB2_BACAN

Accession

Primary (citable) accession number: Q81W73
Secondary accession number(s): Q6HUC0, Q6KNK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program