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Database: UniProt
Entry: A0A2A2AG74_9BURK
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ID   A0A2A2AG74_9BURK        Unreviewed;       652 AA.
AC   A0A2A2AG74;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   28-JAN-2026, entry version 25.
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:PAT37555.1};
GN   ORFNames=CK625_04500 {ECO:0000313|EMBL:PAT37555.1};
OS   Vandammella animalimorsus.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Comamonadaceae; Vandammella.
OX   NCBI_TaxID=2029117 {ECO:0000313|EMBL:PAT37555.1, ECO:0000313|Proteomes:UP000218054};
RN   [1] {ECO:0000313|EMBL:PAT37555.1, ECO:0000313|Proteomes:UP000218054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML00-0135 {ECO:0000313|EMBL:PAT37555.1,
RC   ECO:0000313|Proteomes:UP000218054};
RA   Bernier A.-M., Bernard K.;
RT   "WGS of Clinical strains of the CDC Group NO-1 linked to zoonotic
RT   infections in humans.";
RL   Submitted (AUG-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAT37555.1}.
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DR   EMBL; NSJB01000002; PAT37555.1; -; Genomic_DNA.
DR   RefSeq; WP_095539123.1; NZ_NSJB01000002.1.
DR   AlphaFoldDB; A0A2A2AG74; -.
DR   Proteomes; UP000218054; Unassembled WGS sequence.
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; ELONGATION FACTOR TU-RELATED; 1.
DR   PANTHER; PTHR43721:SF9; GTP-BINDING PROTEIN 1; 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:PAT37555.1};
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:UP000218054}.
FT   DOMAIN          1..176
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   652 AA;  69977 MW;  4CFB5E59A331B603 CRC64;
     MIIGTAGHID HGKTALVRAL TGVDTDRLPE EKARGISIEL SYAYLPVPGT QQVLGFIDVP
     GHEKFVHTMA AGAVGIDHAL LVIAADDGPM PQTREHLAIL ELLGVRQGCV ALNKADRATP
     ARLAAVQAEV AALLQGTPLA GAPVFATNAL DAADAGLAAL RAHLLDAAQR FPARPSQGLF
     RLAVDRSFTL PGQGTIVTGT VFGGSVRVGD VLRHSPSGQS VRVRSIHAQN QPAQAGHSGQ
     RVALNLAGIE RTAIARGDWM AEPQALQATR RLDVQLRVLA SQPQPINPSG QTEASAAKPI
     GPWTSVHLHL GTAHRTAHVV PLEGSHIACG QQARAQLVLD EEVFVTAGDR FILRNAQASQ
     TIAGGQVLDP NAPERKRRSP ERMAYLDAVQ TAIDTGDIAP LIGQAPWGMG RAQLARLLGQ
     PARSLPAPPG CIALGADEAE QLLLAPQHWA ALQAKVCEAL ARFHERTPDE PGVNAARLRR
     MALPNLPPAA LQSPDTLWRG LLAALLEQGL LAQTGPWLHL PSHRVQLSAQ EEQRAAQLLP
     AIAAGRFDPP WVRDLAQAHQ LPEEEVRQLL RKLARQGRLH QVVKDLFYSP EAIDALLAIA
     AELARQSPQQ AVQARHFRDA TALGRKRAIQ VLEYFDRSGH TRRIRDAHVM RT
//
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