ID A9KE35_COXBN Unreviewed; 148 AA.
AC A9KE35;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaE {ECO:0000256|ARBA:ARBA00019010};
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE {ECO:0000256|ARBA:ARBA00032441};
GN OrderedLocusNames=CBUD_1190 {ECO:0000313|EMBL:ABS77308.1};
OS Coxiella burnetii (strain Dugway 5J108-111).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434922 {ECO:0000313|EMBL:ABS77308.1, ECO:0000313|Proteomes:UP000008555};
RN [1] {ECO:0000313|EMBL:ABS77308.1, ECO:0000313|Proteomes:UP000008555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dugway 5J108-111 {ECO:0000313|EMBL:ABS77308.1,
RC ECO:0000313|Proteomes:UP000008555};
RX PubMed=19047403; DOI=10.1128/IAI.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J.III., Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TsaE family.
CC {ECO:0000256|ARBA:ARBA00007599}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000733; ABS77308.1; -; Genomic_DNA.
DR AlphaFoldDB; A9KE35; -.
DR KEGG; cbd:CBUD_1190; -.
DR HOGENOM; CLU_087829_2_2_6; -.
DR Proteomes; UP000008555; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003442; T6A_TsaE.
DR NCBIfam; TIGR00150; T6A_YjeE; 1.
DR PANTHER; PTHR33540; TRNA THREONYLCARBAMOYLADENOSINE BIOSYNTHESIS PROTEIN TSAE; 1.
DR PANTHER; PTHR33540:SF2; TRNA THREONYLCARBAMOYLADENOSINE BIOSYNTHESIS PROTEIN TSAE; 1.
DR Pfam; PF02367; TsaE; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000313|EMBL:ABS77308.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
SQ SEQUENCE 148 AA; 16780 MW; 6A9F4950A756FD89 CRC64;
MLIQKNIPTE KAMLALGQRL ADYCQAGEVI YLMGELGAGK TTFVRGLLRG FGYKGFVKSP
SYTLIEVYSL ETLEVVHVDL YRLSEANEYW DIGLTDYLKK DSILLIEWPE KAEKLLPPPS
VCIHFDIQLN NRLVNITSDS PRLKNISI
//
