ID Q8EKI7_SHEON Unreviewed; 671 AA.
AC Q8EKI7;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 28-JAN-2026, entry version 141.
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:AAN53193.2};
GN OrderedLocusNames=SO_0106 {ECO:0000313|EMBL:AAN53193.2};
OS Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG
OS 19005 / NCIMB 14063 / MR-1).
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Alteromonadales; Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN53193.2, ECO:0000313|Proteomes:UP000008186};
RN [1] {ECO:0000313|EMBL:AAN53193.2, ECO:0000313|Proteomes:UP000008186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063
RC / MR-1 {ECO:0000313|Proteomes:UP000008186};
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [2] {ECO:0000313|EMBL:AAN53193.2, ECO:0000313|Proteomes:UP000008186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063
RC / MR-1 {ECO:0000313|Proteomes:UP000008186};
RX PubMed=16038018; DOI=10.1002/pmic.200401140;
RA Elias D.A., Monroe M.E., Marshall M.J., Romine M.F., Belieav A.S.,
RA Fredrickson J.K., Anderson G.A., Smith R.D., Lipton M.S.;
RT "Global detection and characterization of hypothetical proteins in
RT Shewanella oneidensis MR-1 using LC-MS based proteomics.";
RL Proteomics 5:3120-3130(2005).
RN [3] {ECO:0000313|EMBL:AAN53193.2, ECO:0000313|Proteomes:UP000008186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063
RC / MR-1 {ECO:0000313|Proteomes:UP000008186};
RX PubMed=18378659; DOI=10.1128/AEM.02720-07;
RA Romine M.F., Carlson T.S., Norbeck A.D., McCue L.A., Lipton M.S.;
RT "Identification of mobile elements and pseudogenes in the Shewanella
RT oneidensis MR-1 genome.";
RL Appl. Environ. Microbiol. 74:3257-3265(2008).
RN [4] {ECO:0000313|EMBL:AAN53193.2, ECO:0000313|Proteomes:UP000008186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063
RC / MR-1 {ECO:0000313|Proteomes:UP000008186};
RX PubMed=21810203; DOI=10.1186/1471-2164-12-S1-S1;
RA Romine M.F.;
RT "Genome-wide protein localization prediction strategies for gram negative
RT bacteria.";
RL BMC Genomics 12:S1-S1(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; AE014299; AAN53193.2; -; Genomic_DNA.
DR AlphaFoldDB; Q8EKI7; -.
DR STRING; 211586.SO_0106; -.
DR PaxDb; 211586-SO_0106; -.
DR KEGG; son:SO_0106; -.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_2_0_6; -.
DR OrthoDB; 9803139at2; -.
DR PhylomeDB; Q8EKI7; -.
DR BioCyc; SONE211586:G1GMP-102-MONOMER; -.
DR Proteomes; UP000008186; Chromosome.
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:0035368; F:selenocysteine insertion sequence binding; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0001514; P:selenocysteine incorporation; IBA:GO_Central.
DR GO; GO:0016259; P:selenocysteine metabolic process; IBA:GO_Central.
DR CDD; cd04171; SelB; 1.
DR CDD; cd03696; SelB_II; 1.
DR FunFam; 3.40.50.300:FF:001064; 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; 3.
DR InterPro; IPR057335; Beta-barrel_SelB.
DR InterPro; IPR050543; eIF2G.
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; PTHR42854; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3 FAMILY MEMBER; 1.
DR PANTHER; PTHR42854:SF3; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3-RELATED; 1.
DR Pfam; PF25461; Beta-barrel_SelB; 1.
DR Pfam; PF00009; GTP_EFTU; 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.
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:AAN53193.2};
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:UP000008186}.
FT DOMAIN 1..169
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 671 AA; 74734 MW; C131AC88613C9FDB CRC64;
MVTAGHVDHG KSTLIRALTG MNTDRLPEEK RRGMTIDLGY AFMPLRDGTR LAFIDVPGHE
KFINNMLVGV SHVRHALLVL ACDDGVMPQT REHLQILALL PLNSLTLVLT KRDLVDDQTA
AKLASEGITL LAEYGIEASG VFEVCASDAG DAGVETLKQH ILDIAEQQST QAEDASSFRM
TLDRAFSVKG VGCVVTGTVI SGSVCVGDSL YSSGQKAKLR VRGIHCQGME VHRALSGTRV
ALNLTGVDNH RAPARGDWLS SLPQADLCAR PVVHIRSFEP LTHWQNVHCH HGADHTLGRV
SLLDEADGQG RYLAEIVLDK PLLLCQDDPI VLRHIGGKQT LGAGRVLALK VSNRKKRTPE
RVSKLQQLAQ LTNPVNVLAL LGQSEALSID EIRWRWQLTD EGLAAMLAQA GLTRIGAYGL
STQLLEQEKQ QFIDLLREYH QEHPDQLGLG RNRLQRMSHS VLPSELANKV LDSLCQEGQM
ALRGALLQLA DHRIVLDSEA QQCWQRLAPW LAQQTSPVWV TEMGEYLDLE PAKLRLLCFQ
LVQQGFITAV VKDRYLLSEQ LCHYANLVRE HVDTHGKLET AEFKDMIGLG RKVSIQLLEF
FDRSGFTRRK FRSNSREIRD GELFYSHENW RKNIGVEPTQ DCWQPYPDLK SGRLTGDDVL
PIEDNLIVEN V
//
