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Database: UniProt
Entry: E9CKZ6_9GAMM
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Original site: E9CKZ6_9GAMM 
ID   E9CKZ6_9GAMM            Unreviewed;       572 AA.
AC   E9CKZ6;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   28-JAN-2026, entry version 61.
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:EFW12817.1};
GN   ORFNames=SSYM_0862 {ECO:0000313|EMBL:EFW12817.1};
OS   Serratia symbiotica str. Tucson.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Yersiniaceae; Serratia; Serratia symbiotica.
OX   NCBI_TaxID=914128 {ECO:0000313|EMBL:EFW12817.1, ECO:0000313|Proteomes:UP000013568};
RN   [1] {ECO:0000313|Proteomes:UP000013568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson {ECO:0000313|Proteomes:UP000013568};
RX   PubMed=21266540;
RA   Burke G.R., Moran N.A.;
RT   "Massive genomic decay in Serratia symbiotica, a recently evolved symbiont
RT   of aphids.";
RL   Genome Biol. Evol. 3:195-208(2011).
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; GL636105; EFW12817.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9CKZ6; -.
DR   HOGENOM; CLU_023030_2_0_6; -.
DR   Proteomes; UP000013568; 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:InterPro.
DR   GO; GO:0001514; P:selenocysteine incorporation; IEA:InterPro.
DR   CDD; cd03696; SelB_II; 1.
DR   FunFam; 1.10.10.10:FF:000350; Selenocysteine-specific translation elongation factor; 1.
DR   FunFam; 2.40.30.10:FF:000080; Selenocysteine-specific translation elongation factor; 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; 2.
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; 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; IPR048649; WHD_1st_3rd_SelB.
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; PF21458; WHD_1st_3rd_SelB; 1.
DR   Pfam; PF09106; WHD_2nd_SelB; 1.
DR   Pfam; PF21214; WHD_2nd_SelB_bact; 1.
DR   Pfam; PF09107; WHD_3rd_SelB; 1.
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; 2.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000013568}.
FT   DOMAIN          14..125
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|Pfam:PF00009"
FT   DOMAIN          148..215
FT                   /note="Translation elongation factor EFTu-like"
FT                   /evidence="ECO:0000259|Pfam:PF03144"
FT   DOMAIN          225..303
FT                   /note="Selenocysteine-specific elongation factor beta-
FT                   barrel"
FT                   /evidence="ECO:0000259|Pfam:PF25461"
FT   DOMAIN          309..356
FT                   /note="Selenocysteine-specific elongation factor first
FT                   winged helix"
FT                   /evidence="ECO:0000259|Pfam:PF21458"
FT   DOMAIN          383..439
FT                   /note="Translation elongation factor SelB winged helix type
FT                   2"
FT                   /evidence="ECO:0000259|Pfam:PF09106"
FT   DOMAIN          446..504
FT                   /note="Selenocysteine-specific elongation factor second
FT                   winged helix"
FT                   /evidence="ECO:0000259|Pfam:PF21214"
FT   DOMAIN          523..564
FT                   /note="Elongation factor SelB fourth winged-helix"
FT                   /evidence="ECO:0000259|Pfam:PF09107"
SQ   SEQUENCE   572 AA;  62892 MW;  8341CA9FB5DFF86F CRC64;
     MPTGHNLMAE CWGFIDVPGH EKFLANMLAG VGGIDHALLV VACDDGVMAQ TREHLAILRL
     SGRLVLTVAL TKADRVDGAR IDVVCQQVQE ELARQGWHPT PLFVTAAVQG TGIKALCEHL
     QTLLPGDHGL TRRFRLAVDR AFSIKGAGLV VTGTALGGRV TVGETLWLTG ADTPVRVRGL
     HAQNQPVKQA QAGQRIALNI SGDVSKEQIA RGDWLLSHRP LAAAERILVA LDADLPIRHK
     QPLHLHHAAS HITGRISLLN DNLAELILDR PLWLVENDRL VLRDIGARQT LGAAQVLSLS
     VPKRGKRSPC FLVRLAAQAQ ASDDRQALAL LLSQGALQIA AFSWARQLTD SGLANLLAQH
     QLLIAGGSAL AIDKVQQAES RLLQILADYH QQHADQLGLG RARLRRMALR ALDEALVFKM
     IDNLLHIGAI SHTRGWLHLP EHALTFSTEE MAFWERIVPL FGGEAWWVRD LAAELGEDEV
     RVRTLLRKAA LLDHVTAVVV DRYYLSSCIE QFAALIRELN VTQGSVNAVD FRDRLGIGRK
     LAIQVLEFFD RSGFTRRKGN QHLLRDHGLF SE
//
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