TSAB_THEMA
ID TSAB_THEMA Reviewed; 206 AA.
AC Q9WZX7; G4FCV1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaB;
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB;
GN Name=tsaB; OrderedLocusNames=TM_0874; ORFNames=Tmari_0876;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485;
RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
RA Zengler K.;
RT "The genome organization of Thermotoga maritima reflects its lifestyle.";
RL PLoS Genet. 9:E1003485-E1003485(2013).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), AND SUBUNIT.
RX PubMed=20944216; DOI=10.1107/s1744309109022192;
RA Xu Q., McMullan D., Jaroszewski L., Krishna S.S., Elsliger M.A., Yeh A.P.,
RA Abdubek P., Astakhova T., Axelrod H.L., Carlton D., Chiu H.J., Clayton T.,
RA Duan L., Feuerhelm J., Grant J., Han G.W., Jin K.K., Klock H.E.,
RA Knuth M.W., Miller M.D., Morse A.T., Nigoghossian E., Okach L.,
RA Oommachen S., Paulsen J., Reyes R., Rife C.L., van den Bedem H.,
RA Hodgson K.O., Wooley J., Deacon A.M., Godzik A., Lesley S.A., Wilson I.A.;
RT "Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga
RT maritima at 2.5 A resolution.";
RL Acta Crystallogr. F 66:1230-1236(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS), AND SUBUNIT.
RX PubMed=29741707; DOI=10.1093/nar/gky323;
RA Missoury S., Plancqueel S., Li de la Sierra-Gallay I., Zhang W., Liger D.,
RA Durand D., Dammak R., Collinet B., van Tilbeurgh H.;
RT "The structure of the TsaB/TsaD/TsaE complex reveals an unexpected
RT mechanism for the bacterial t6A tRNA-modification.";
RL Nucleic Acids Res. 46:5850-5860(2018).
CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC with adenine. Is involved in the transfer of the threonylcarbamoyl
CC moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37,
CC together with TsaD and TsaE; this reaction does not require ATP in
CC vitro. TsaB seems to play an indirect role in the t(6)A biosynthesis
CC pathway, possibly in regulating the core enzymatic function of TsaD (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (PubMed:20944216). Forms an hexamer composed of two
CC TsaB, TsaD and TsaE trimers (PubMed:29741707).
CC {ECO:0000269|PubMed:20944216, ECO:0000269|PubMed:29741707}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. TsaB subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD35955.1; -; Genomic_DNA.
DR EMBL; CP004077; AGL49801.1; -; Genomic_DNA.
DR PIR; D72323; D72323.
DR RefSeq; NP_228682.1; NC_000853.1.
DR RefSeq; WP_004080725.1; NZ_CP011107.1.
DR PDB; 2A6A; X-ray; 2.50 A; A/B=1-206.
DR PDB; 6N9A; X-ray; 2.50 A; B=2-206.
DR PDB; 6S84; X-ray; 2.89 A; C/F=1-206.
DR PDBsum; 2A6A; -.
DR PDBsum; 6N9A; -.
DR PDBsum; 6S84; -.
DR AlphaFoldDB; Q9WZX7; -.
DR SMR; Q9WZX7; -.
DR STRING; 243274.THEMA_00265; -.
DR DNASU; 898547; -.
DR EnsemblBacteria; AAD35955; AAD35955; TM_0874.
DR EnsemblBacteria; AGL49801; AGL49801; Tmari_0876.
DR KEGG; tma:TM0874; -.
DR KEGG; tmm:Tmari_0876; -.
DR KEGG; tmw:THMA_0896; -.
DR PATRIC; fig|243274.17.peg.875; -.
DR eggNOG; COG1214; Bacteria.
DR InParanoid; Q9WZX7; -.
DR OMA; ELNWERK; -.
DR OrthoDB; 1826274at2; -.
DR EvolutionaryTrace; Q9WZX7; -.
DR Proteomes; UP000008183; Chromosome.
DR Proteomes; UP000013901; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR022496; T6A_TsaB.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF11; PTHR11735:SF11; 1.
DR Pfam; PF00814; TsaD; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR03725; T6A_YeaZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; tRNA processing.
FT CHAIN 1..206
FT /note="tRNA threonylcarbamoyladenosine biosynthesis protein
FT TsaB"
FT /id="PRO_0000423848"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2A6A"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:2A6A"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:2A6A"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:2A6A"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:2A6A"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2A6A"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2A6A"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6S84"
FT HELIX 67..81
FT /evidence="ECO:0007829|PDB:2A6A"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2A6A"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2A6A"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:2A6A"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6N9A"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:2A6A"
FT STRAND 117..128
FT /evidence="ECO:0007829|PDB:2A6A"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:2A6A"
FT HELIX 140..150
FT /evidence="ECO:0007829|PDB:2A6A"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:2A6A"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:2A6A"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2A6A"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:2A6A"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:6N9A"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:6N9A"
SQ SEQUENCE 206 AA; 22987 MW; F5A341FBA22E66E7 CRC64;
MNVLALDTSQ RIRIGLRKGE DLFEISYTGE KKHAEILPVV VKKLLDELDL KVKDLDVVGV
GIGPGGLTGL RVGIATVVGL VSPYDIPVAP LNSFEMTAKS CPADGVVLVA RRARKGYHYC
AVYLKDKGLN PLKEPSVVSD EELEEITKEF SPKIVLKDDL LISPAVLVEE SERLFREKKT
IHYYEIEPLY LQKSIAELNW EKKKRG
