TSAE_HAEIN
ID TSAE_HAEIN Reviewed; 158 AA.
AC P44492;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaE;
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE;
GN Name=tsaE; Synonyms=yjeE; OrderedLocusNames=HI_0065;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF APOPROEIN AND IN COMPLEX WITH
RP MG-ADP, FUNCTION, ATPASE ACTIVITY, AND KINETIC PARAMETERS.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=12112691; DOI=10.1002/prot.10114;
RA Teplyakov A., Obmolova G., Tordova M., Thanki N., Bonander N.,
RA Eisenstein E., Howard A.J., Gilliland G.L.;
RT "Crystal structure of the YjeE protein from Haemophilus influenzae: a
RT putative Atpase involved in cell wall synthesis.";
RL Proteins 48:220-226(2002).
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 TsaB. TsaE seems to play an indirect role in the
CC t(6)A biosynthesis pathway, possibly in regulating the core enzymatic
CC function of TsaD (By similarity). Displays ATPase activity in vitro.
CC {ECO:0000250, ECO:0000269|PubMed:12112691}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=38 uM for ATP {ECO:0000269|PubMed:12112691};
CC Note=kcat is 0.42 min(-1) for ATP hydrolysis.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TsaE family. {ECO:0000305}.
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DR EMBL; L42023; AAC21743.1; -; Genomic_DNA.
DR PIR; H64141; H64141.
DR RefSeq; NP_438238.1; NC_000907.1.
DR RefSeq; WP_005693857.1; NC_000907.1.
DR PDB; 1FL9; X-ray; 2.50 A; A/B/C=1-158.
DR PDB; 1HTW; X-ray; 1.70 A; A/B/C=1-158.
DR PDBsum; 1FL9; -.
DR PDBsum; 1HTW; -.
DR AlphaFoldDB; P44492; -.
DR SMR; P44492; -.
DR STRING; 71421.HI_0065; -.
DR EnsemblBacteria; AAC21743; AAC21743; HI_0065.
DR KEGG; hin:HI_0065; -.
DR PATRIC; fig|71421.8.peg.66; -.
DR eggNOG; COG0802; Bacteria.
DR HOGENOM; CLU_087829_2_2_6; -.
DR OMA; FTDDAIC; -.
DR PhylomeDB; P44492; -.
DR BioCyc; HINF71421:G1GJ1-66-MON; -.
DR EvolutionaryTrace; P44492; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003442; T6A_TsaE.
DR Pfam; PF02367; TsaE; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00150; T6A_YjeE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; tRNA processing.
FT CHAIN 1..158
FT /note="tRNA threonylcarbamoyladenosine biosynthesis protein
FT TsaE"
FT /id="PRO_0000096208"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 43..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1HTW"
FT HELIX 11..28
FT /evidence="ECO:0007829|PDB:1HTW"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1HTW"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:1HTW"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1HTW"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1HTW"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1HTW"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1HTW"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:1HTW"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1HTW"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1HTW"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:1HTW"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:1HTW"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:1HTW"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:1HTW"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:1HTW"
SQ SEQUENCE 158 AA; 17970 MW; D148C82B95610FCD CRC64;
MESLTQYIPD EFSMLRFGKK FAEILLKLHT EKAIMVYLNG DLGAGKTTLT RGMLQGIGHQ
GNVKSPTYTL VEEYNIAGKM IYHFDLYRLA DPEELEFMGI RDYFNTDSIC LIEWSEKGQG
ILPEADILVN IDYYDDARNI ELIAQTNLGK NIISAFSN
