ID A0A7Z2G7F7_9BURK Unreviewed; 642 AA.
AC A0A7Z2G7F7;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN Name=selB {ECO:0000313|EMBL:QGZ56596.1};
GN ORFNames=FAZ97_16620 {ECO:0000313|EMBL:QGZ56596.1};
OS Paraburkholderia acidiphila.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2571747 {ECO:0000313|EMBL:QGZ56596.1, ECO:0000313|Proteomes:UP000434209};
RN [1] {ECO:0000313|EMBL:QGZ56596.1, ECO:0000313|Proteomes:UP000434209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7Q-K02 {ECO:0000313|EMBL:QGZ56596.1,
RC ECO:0000313|Proteomes:UP000434209};
RA Gao Z., Qiu L.;
RT "Paraburkholderia acidiphila 7Q-K02 sp. nov and Paraburkholderia acidisoli
RT DHF22 sp. nov., two strains isolated from forest soil.";
RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Translation factor necessary for the incorporation of
CC selenocysteine into proteins. It probably replaces EF-Tu for the
CC insertion of selenocysteine directed by the UGA codon. SelB binds GTP
CC and GDP. {ECO:0000256|ARBA:ARBA00025526}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP046910; QGZ56596.1; -; Genomic_DNA.
DR RefSeq; WP_158759552.1; NZ_CP046910.1.
DR AlphaFoldDB; A0A7Z2G7F7; -.
DR KEGG; pacp:FAZ97_16620; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000434209; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0001514; P:selenocysteine incorporation; IEA:InterPro.
DR CDD; cd04171; SelB; 1.
DR CDD; cd03696; SelB_II; 1.
DR CDD; cd15491; selB_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 3.
DR InterPro; IPR057335; Beta-barrel_SelB.
DR InterPro; IPR050055; EF-Tu_GTPase.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015191; SelB_WHD4.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004535; Transl_elong_SelB.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR048931; WHD_2nd_SelB_bact.
DR NCBIfam; TIGR00475; selB; 1.
DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR Pfam; PF25461; Beta-barrel_SelB; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF09106; WHD_2nd_SelB; 1.
DR Pfam; PF21214; WHD_2nd_SelB_bact; 1.
DR Pfam; PF09107; WHD_3rd_SelB; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 3.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:QGZ56596.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000434209}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 642 AA; 70035 MW; 48B2AF592D4D3F7F CRC64;
MIVGTAGHID HGKTTLVRAL TGVDTDRLKE EKARGISIEL GYAYLPLANG DVLGFIDVPG
HEKLVHTMAA GACGIDFALL VIAADDGVMP QTREHLAILQ LLGVQQGAIA LTKADRVDVA
RLDAVRAEIA AWLAETMFAD APIFETNATQ PHDEGVARLD AWLRERASTW RARRDDGLFR
LAVDRVFTLT GQGTVVTGTV FSGRVQAGDA LVLAPAGTSV RVRGLHAQNR AVPAGNAGHA
GQRCALNLAG IDKGQIARGD WIVDARLAEP AMRLDVELQL LGDADITLQH WSPLHVHLGT
THRVVNVALL EGETLGPGAA ARVQLVFDAP LHAMPGDRFI VRNAQANRTI GGGRVLDPFG
PPRRRRTAER RAWLDAMRTW LDEANLAPLI DEAPRGIART TLVRLTGYDD AALALPADAI
SIAPQGRDDE GALIAHAHWT KLTGRIVEAL GEFHARSPDE QGPDAARLRR MAAPLVSDAV
WRAAIEALER EGRVARSGPW LHLPSHAVTL DADDEALAAR LMPLVAQGRF DPPWVRDLAR
ETGQPEERVR ALLRKLARLG RVYQVVRDLF YDRDVVQTLA RAVAQIAAEQ DGAVNAAAFR
DATALGRKRA IQILEYFDRV GYTRFQRDTH LLRHDSRMRE WL
//
