ID   EFTS_BARQU              Reviewed;         307 AA.
AC   Q9XCM5; Q6FZN1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Elongation factor Ts;
DE            Short=EF-Ts;
GN   Name=tsf; OrderedLocusNames=BQ07000;
OS   Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51694 / 90-268;
RA   Marston E.L., Eldeieef S., Regnery R.L.;
RT   "Cloning and characterization of elongation factor-ts (EF-ts) gene from
RT   Bartonella quintana.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
CC   -!- FUNCTION: Associates with the EF-Tu.GDP complex and induces the
CC       exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-
CC       Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000305}.
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DR   EMBL; AF138286; AAD39149.1; -; Genomic_DNA.
DR   EMBL; BX897700; CAF26189.1; -; Genomic_DNA.
DR   RefSeq; WP_011179444.1; NC_005955.1.
DR   AlphaFoldDB; Q9XCM5; -.
DR   SMR; Q9XCM5; -.
DR   STRING; 283165.BQ07000; -.
DR   EnsemblBacteria; CAF26189; CAF26189; BQ07000.
DR   KEGG; bqu:BQ07000; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_2_0_5; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000000597; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.479.20; -; 2.
DR   HAMAP; MF_00050; EF_Ts; 1.
DR   InterPro; IPR036402; EF-Ts_dimer_sf.
DR   InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR   InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR   InterPro; IPR018101; Transl_elong_Ts_CS.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR11741; PTHR11741; 1.
DR   Pfam; PF00889; EF_TS; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54713; SSF54713; 1.
DR   TIGRFAMs; TIGR00116; tsf; 1.
DR   PROSITE; PS01127; EF_TS_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis.
FT   CHAIN           1..307
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161081"
FT   REGION          79..82
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        122
FT                   /note="E -> Q (in Ref. 1; AAD39149)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        300
FT                   /note="E -> K (in Ref. 1; AAD39149)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   307 AA;  32455 MW;  47B1F316699E2863 CRC64;
     MSITAAQVKE LRELSGAGMM DCKAALADTN GDMEAAVDWL RKKGIAKADK KAGRTAAEGL
     IGIVSKDTSA VLVEINSETD FVARNDLFQD IVRNVATAAL DTQGNVESVS ASFYPGSEKT
     VEATIKDAIS TIGENMTFRR SAKLSVKDGV VATYIHSKVA EGLGKLGVLV AVETTGNKEA
     AAVFGRQVAM HIAATNPLAL TAEDVDSGAV EREKAIFSDQ ARQSGKPENI IEKMVEGRLR
     KFFEEVVLLS QAFVMNPDIT VEAALKDAEK SIGAPARITG FIRFALGEGV EKKESNFAAE
     VAAAAKG