O31663 (MTNK_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methylthioribose kinase
Short name=MTR kinase
EC=2.7.1.100

Gene names

Name:	mtnK
Synonyms:	ykrT
Ordered Locus Names:	BSU13560

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate. Ref.2
Catalytic activity	ATP + S-methyl-5-thio-D-ribose = ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate. HAMAP MF_01683
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 2/2. HAMAP MF_01683
Subunit structure	Homodimer. Ref.4 Ref.5
Induction	By starvation. HAMAP MF_01683
Sequence similarities	Belongs to the methylthioribose kinase family.
Sequence caution	The sequence CAB13229.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis Stress response
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW S-methyl-5-thioribose kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 397

397

Methylthioribose kinase HAMAP MF_01683

PRO_0000162915

Regions

Nucleotide binding

115 – 117

3

ATP HAMAP MF_01683

Nucleotide binding

250 – 252

3

ATP HAMAP MF_01683

Sites

Binding site

44

1

ATP

Binding site

61

1

ATP

Binding site

233

1

Substrate

Binding site

340

1

Substrate

Secondary structure

1

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397

Helix Strand Turn

Details...

Helix

14 – 23

10

Beta strand

34 – 37

4

Beta strand

40 – 50

11

Beta strand

57 – 63

7

Helix

80 – 92

13

Helix

96 – 98

3

Beta strand

102 – 106

5

Turn

107 – 110

4

Beta strand

111 – 114

4

Beta strand

120 – 122

3

Helix

123 – 128

6

Helix

136 – 150

15

Turn

153 – 155

3

Helix

158 – 167

10

Helix

171 – 180

10

Turn

181 – 183

3

Helix

184 – 186

3

Helix

196 – 198

3

Helix

199 – 206

8

Helix

209 – 224

16

Beta strand

228 – 230

3

Helix

236 – 238

3

Beta strand

239 – 241

3

Beta strand

246 – 248

3

Beta strand

255 – 257

3

Helix

260 – 276

17

Helix

279 – 282

4

Helix

283 – 307

25

Turn

311 – 314

4

Helix

318 – 343

26

Beta strand

344 – 346

3

Helix

349 – 352

4

Helix

357 – 377

21

Turn

378 – 380

3

Helix

384 – 394

11

Sequences

	Sequence		Length	Mass (Da)
	O31663 [UniParc]. Last modified October 24, 2003. Version 2. Checksum: E5862F8D8492189C	FASTA	397	45,085
	10 20 30 40 50 60 MGVTKTPLYE TLNESSAVAL AVKLGLFPSK STLTCQEIGD GNLNYVFHIY DQEHDRALII 70 80 90 100 110 120 KQAVPYAKVV GESWPLTIDR ARIESSALIR QGEHVPHLVP RVFYSDTEMA VTVMEDLSHL 130 140 150 160 170 180 KIARKGLIEG ENYPHLSQHI GEFLGKTLFY SSDYALEPKV KKQLVKQFTN PELCDITERL 190 200 210 220 230 240 VFTDPFFDHD TNDFEEELRP FVEKLWNNDS VKIEAAKLKK SFLTSAETLI HGDLHTGSIF 250 260 270 280 290 300 ASEHETKVID PEFAFYGPIG FDVGQFIANL FLNALSRDGA DREPLYEHVN QVWETFEETF 310 320 330 340 350 360 SEAWQKDSLD VYANIDGYLT DTLSHIFEEA IGFAGCELIR RTIGLAHVAD LDTIVPFDKR 370 380 390 IGRKRLALET GTAFIEKRSE FKTITDVIEL FKLLVKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[2]	"MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis." Sekowska A., Mulard L., Krogh S., Tse J.K.S., Danchin A. BMC Microbiol. 1:15-15(2001) [PubMed: 11545674] [Abstract] Cited for: FUNCTION, REANALYSIS OF N-TERMINUS.
[3]	"The methionine salvage pathway in Bacillus subtilis." Sekowska A., Danchin A. BMC Microbiol. 2:8-8(2002) [PubMed: 12022921] [Abstract] Cited for: REVIEW.
[4]	"ADP-2Ho as a phasing tool for nucleotide-containing proteins." Ku S.-Y., Smith G.D., Howell P.L. Acta Crystallogr. D 63:493-499(2007) [PubMed: 17372354] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP-2HO, SUBUNIT.
[5]	"Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding." Ku S.Y., Yip P., Cornell K.A., Riscoe M.K., Behr J.B., Guillerm G., Howell P.L. J. Biol. Chem. 282:22195-22206(2007) [PubMed: 17522047] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMLEX WITH ADENOSYL NUCLEOTIDES AND SUBSTRATE ANALOGS, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL009126 Genomic DNA. Translation: CAB13229.1. Different initiation.

PIR

D69863.

RefSeq

NP_389239.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OLC	X-ray	2.00	A/B	1-397	[»]
2PU8	X-ray	2.10	A/B	1-397	[»]
2PUI	X-ray	2.20	A/B	1-397	[»]
2PUL	X-ray	2.00	A/B	1-397	[»]
2PUN	X-ray	2.30	A/B	1-397	[»]
2PUP	X-ray	2.60	A/B	1-397	[»]

ProteinModelPortal

O31663.

SMR

O31663. Positions 5-396.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000002189; EBBACP00000002189; EBBACG00000002186.

GeneID

939336.

GenomeReviews

Gene locus BSU13560 in contig AL009126_GR.

KEGG

bsu:BSU13560.

NMPDR

fig|224308.1.peg.1358.

PATRIC

18974480. VBIBacSub10457_1432.

Organism-specific databases

GenoList

BSU13560. [Micado]

Phylogenomic databases

GeneTree

EBGT00050000001231.

HOGENOM

HBG305135.

PhylomeDB

O31663.

ProtClustDB

PRK09550.

Enzyme and pathway databases

BioCyc

BSUB:BSU13560-MONOMER.

Family and domain databases

HAMAP

MF_01683. Salvage_MtnK.
[Tree]

InterPro

IPR002575. Aminoglycoside_PTrfase.
IPR011009. Kinase-like_dom.
IPR009212. Methylthioribose_kinase.
[Graphical view]

KO

K00899.

Pfam

PF01636. APH. 1 hit.
[Graphical view]

PIRSF

PIRSF031134. MTRK. 1 hit.

SUPFAM

SSF56112. Kinase_like. 1 hit.

TIGRFAMs

TIGR01767. MTRK. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MTNK_BACSU

Accession

Primary (citable) accession number: O31663

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
Last sequence update:	October 24, 2003
Last modified:	January 25, 2012
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program