MTNK_BACSU
ID MTNK_BACSU Reviewed; 397 AA.
AC O31663;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Methylthioribose kinase {ECO:0000303|PubMed:11545674};
DE Short=MTR kinase {ECO:0000303|PubMed:11545674};
DE EC=2.7.1.100 {ECO:0000269|PubMed:11545674};
GN Name=mtnK; Synonyms=ykrT; OrderedLocusNames=BSU13560;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND REANALYSIS OF N-TERMINUS.
RX PubMed=11545674; DOI=10.1186/1471-2180-1-15;
RA Sekowska A., Mulard L., Krogh S., Tse J.K.S., Danchin A.;
RT "MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus
RT subtilis.";
RL BMC Microbiol. 1:15-15(2001).
RN [3]
RP REVIEW.
RX PubMed=12022921; DOI=10.1186/1471-2180-2-8;
RA Sekowska A., Danchin A.;
RT "The methionine salvage pathway in Bacillus subtilis.";
RL BMC Microbiol. 2:8-8(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP-2HO, AND SUBUNIT.
RX PubMed=17372354; DOI=10.1107/s0907444907006592;
RA Ku S.-Y., Smith G.D., Howell P.L.;
RT "ADP-2Ho as a phasing tool for nucleotide-containing proteins.";
RL Acta Crystallogr. D 63:493-499(2007).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ADENOSYL NUCLEOTIDES
RP AND SUBSTRATE ANALOGS, AND SUBUNIT.
RX PubMed=17522047; DOI=10.1074/jbc.m611045200;
RA Ku S.Y., Yip P., Cornell K.A., Riscoe M.K., Behr J.B., Guillerm G.,
RA Howell P.L.;
RT "Structures of 5-methylthioribose kinase reveal substrate specificity and
RT unusual mode of nucleotide binding.";
RL J. Biol. Chem. 282:22195-22206(2007).
CC -!- FUNCTION: Catalyzes the phosphorylation of methylthioribose into
CC methylthioribose-1-phosphate. {ECO:0000269|PubMed:11545674}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-(methylsulfanyl)-D-ribose + ATP = ADP + H(+) + S-methyl-5-
CC thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:22312,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58533,
CC ChEBI:CHEBI:78440, ChEBI:CHEBI:456216; EC=2.7.1.100;
CC Evidence={ECO:0000269|PubMed:11545674};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-
CC thioadenosine (hydrolase route): step 2/2.
CC {ECO:0000305|PubMed:11545674}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17372354,
CC ECO:0000269|PubMed:17522047}.
CC -!- INDUCTION: By starvation. {ECO:0000269|PubMed:11545674}.
CC -!- SIMILARITY: Belongs to the methylthioribose kinase family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB13229.2; -; Genomic_DNA.
DR PIR; D69863; D69863.
DR RefSeq; NP_389239.1; NC_000964.3.
DR RefSeq; WP_003244973.1; NZ_JNCM01000035.1.
DR PDB; 2OLC; X-ray; 2.00 A; A/B=1-397.
DR PDB; 2PU8; X-ray; 2.10 A; A/B=1-397.
DR PDB; 2PUI; X-ray; 2.20 A; A/B=1-397.
DR PDB; 2PUL; X-ray; 2.00 A; A/B=1-397.
DR PDB; 2PUN; X-ray; 2.30 A; A/B=1-397.
DR PDB; 2PUP; X-ray; 2.60 A; A/B=1-397.
DR PDBsum; 2OLC; -.
DR PDBsum; 2PU8; -.
DR PDBsum; 2PUI; -.
DR PDBsum; 2PUL; -.
DR PDBsum; 2PUN; -.
DR PDBsum; 2PUP; -.
DR AlphaFoldDB; O31663; -.
DR SMR; O31663; -.
DR IntAct; O31663; 1.
DR MINT; O31663; -.
DR STRING; 224308.BSU13560; -.
DR PaxDb; O31663; -.
DR PRIDE; O31663; -.
DR EnsemblBacteria; CAB13229; CAB13229; BSU_13560.
DR GeneID; 939336; -.
DR KEGG; bsu:BSU13560; -.
DR PATRIC; fig|224308.179.peg.1473; -.
DR eggNOG; COG4857; Bacteria.
DR InParanoid; O31663; -.
DR OMA; EMCEITE; -.
DR BioCyc; BSUB:BSU13560-MON; -.
DR BRENDA; 2.7.1.100; 658.
DR SABIO-RK; O31663; -.
DR UniPathway; UPA00904; UER00872.
DR EvolutionaryTrace; O31663; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046522; F:S-methyl-5-thioribose kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_01683; Salvage_MtnK; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR009212; Methylthioribose_kinase.
DR Pfam; PF01636; APH; 1.
DR PIRSF; PIRSF031134; MTRK; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR01767; MTRK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Kinase;
KW Methionine biosynthesis; Nucleotide-binding; Reference proteome;
KW Stress response; Transferase.
FT CHAIN 1..397
FT /note="Methylthioribose kinase"
FT /id="PRO_0000162915"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17372354,
FT ECO:0000269|PubMed:17522047"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17372354,
FT ECO:0000269|PubMed:17522047"
FT BINDING 115..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17372354,
FT ECO:0000269|PubMed:17522047"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17522047"
FT BINDING 250..252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17372354,
FT ECO:0000269|PubMed:17522047"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17522047"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:2OLC"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:2OLC"
FT STRAND 40..50
FT /evidence="ECO:0007829|PDB:2OLC"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:2PU8"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2PUL"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:2OLC"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:2OLC"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:2OLC"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:2OLC"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:2OLC"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:2OLC"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 209..224
FT /evidence="ECO:0007829|PDB:2OLC"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:2OLC"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2OLC"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2OLC"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 260..276
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 283..307
FT /evidence="ECO:0007829|PDB:2OLC"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 318..343
FT /evidence="ECO:0007829|PDB:2OLC"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 357..377
FT /evidence="ECO:0007829|PDB:2OLC"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:2OLC"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:2OLC"
SQ SEQUENCE 397 AA; 45085 MW; E5862F8D8492189C CRC64;
MGVTKTPLYE TLNESSAVAL AVKLGLFPSK STLTCQEIGD GNLNYVFHIY DQEHDRALII
KQAVPYAKVV GESWPLTIDR ARIESSALIR QGEHVPHLVP RVFYSDTEMA VTVMEDLSHL
KIARKGLIEG ENYPHLSQHI GEFLGKTLFY SSDYALEPKV KKQLVKQFTN PELCDITERL
VFTDPFFDHD TNDFEEELRP FVEKLWNNDS VKIEAAKLKK SFLTSAETLI HGDLHTGSIF
ASEHETKVID PEFAFYGPIG FDVGQFIANL FLNALSRDGA DREPLYEHVN QVWETFEETF
SEAWQKDSLD VYANIDGYLT DTLSHIFEEA IGFAGCELIR RTIGLAHVAD LDTIVPFDKR
IGRKRLALET GTAFIEKRSE FKTITDVIEL FKLLVKE
