SELB_ECOLI
ID SELB_ECOLI Reviewed; 614 AA.
AC P14081; Q2M7Q3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Selenocysteine-specific elongation factor;
DE AltName: Full=SelB translation factor;
GN Name=selB; Synonyms=fdhA; OrderedLocusNames=b3590, JW3563;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=2531290; DOI=10.1038/342453a0;
RA Forchhammer K., Leinfelder W., Boeck A.;
RT "Identification of a novel translation factor necessary for the
RT incorporation of selenocysteine into protein.";
RL Nature 342:453-456(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP C-TERMINUS.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CHARACTERIZATION.
RX PubMed=2140572; DOI=10.1016/s0021-9258(19)38855-6;
RA Forchhammer K., Rucknagel K.-P., Bock A.;
RT "Purification and biochemical characterization of SELB, a translation
RT factor involved in selenoprotein synthesis.";
RL J. Biol. Chem. 265:9346-9350(1990).
RN [6]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
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.
CC -!- INTERACTION:
CC P14081; P23721: serC; NbExp=3; IntAct=EBI-551705, EBI-557952;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: There are about 1100 copies of SelB per E.coli cell.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. SelB subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; X16644; CAA34637.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18567.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC76614.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77703.1; -; Genomic_DNA.
DR PIR; JV0050; EFECSB.
DR RefSeq; NP_418047.1; NC_000913.3.
DR RefSeq; WP_000582468.1; NZ_SSZK01000041.1.
DR PDB; 2PJP; X-ray; 2.30 A; A=487-607.
DR PDB; 5LZB; EM; 5.30 A; z=1-614.
DR PDB; 5LZC; EM; 4.80 A; z=1-614.
DR PDB; 5LZD; EM; 3.40 A; z=1-614.
DR PDBsum; 2PJP; -.
DR PDBsum; 5LZB; -.
DR PDBsum; 5LZC; -.
DR PDBsum; 5LZD; -.
DR AlphaFoldDB; P14081; -.
DR SMR; P14081; -.
DR BioGRID; 4261875; 9.
DR DIP; DIP-10848N; -.
DR IntAct; P14081; 42.
DR STRING; 511145.b3590; -.
DR jPOST; P14081; -.
DR PaxDb; P14081; -.
DR PRIDE; P14081; -.
DR EnsemblBacteria; AAC76614; AAC76614; b3590.
DR EnsemblBacteria; BAE77703; BAE77703; BAE77703.
DR GeneID; 948103; -.
DR KEGG; ecj:JW3563; -.
DR KEGG; eco:b3590; -.
DR PATRIC; fig|1411691.4.peg.3121; -.
DR EchoBASE; EB0935; -.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_2_0_6; -.
DR InParanoid; P14081; -.
DR OMA; YAIDRVF; -.
DR PhylomeDB; P14081; -.
DR BioCyc; EcoCyc:EG10942-MON; -.
DR BioCyc; MetaCyc:EG10942-MON; -.
DR EvolutionaryTrace; P14081; -.
DR PRO; PR:P14081; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019003; F:GDP binding; IDA:EcoCyc.
DR GO; GO:0005525; F:GTP binding; IDA:EcoCyc.
DR GO; GO:0003924; F:GTPase activity; IDA:EcoCyc.
DR GO; GO:0035368; F:selenocysteine insertion sequence binding; IDA:EcoCyc.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IDA:EcoCyc.
DR GO; GO:0001514; P:selenocysteine incorporation; IMP:EcoCyc.
DR GO; GO:0016259; P:selenocysteine metabolic process; IMP:EcoCyc.
DR Gene3D; 1.10.10.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
DR InterPro; IPR015191; Elong_fac_SelB-wing-hlx_typ-3.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
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 Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF09106; SelB-wing_2; 1.
DR Pfam; PF09107; SelB-wing_3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF46785; SSF46785; 3.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00475; selB; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..614
FT /note="Selenocysteine-specific elongation factor"
FT /id="PRO_0000091474"
FT DOMAIN 1..173
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 7..14
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 35..39
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 57..60
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 112..115
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 147..149
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 7..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 112..115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT HELIX 489..498
FT /evidence="ECO:0007829|PDB:2PJP"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:2PJP"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:2PJP"
FT HELIX 509..515
FT /evidence="ECO:0007829|PDB:2PJP"
FT HELIX 520..532
FT /evidence="ECO:0007829|PDB:2PJP"
FT STRAND 535..540
FT /evidence="ECO:0007829|PDB:2PJP"
FT STRAND 543..546
FT /evidence="ECO:0007829|PDB:2PJP"
FT HELIX 547..564
FT /evidence="ECO:0007829|PDB:2PJP"
FT STRAND 565..568
FT /evidence="ECO:0007829|PDB:2PJP"
FT HELIX 569..576
FT /evidence="ECO:0007829|PDB:2PJP"
FT HELIX 580..592
FT /evidence="ECO:0007829|PDB:2PJP"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:2PJP"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:2PJP"
SQ SEQUENCE 614 AA; 68867 MW; 1C0690A2672FCB1A CRC64;
MIIATAGHVD HGKTTLLQAI TGVNADRLPE EKKRGMTIDL GYAYWPQPDG RVPGFIDVPG
HEKFLSNMLA GVGGIDHALL VVACDDGVMA QTREHLAILQ LTGNPMLTVA LTKADRVDEA
RVDEVERQVK EVLREYGFAE AKLFITAATE GRGMDALREH LLQLPEREHA SQHSFRLAID
RAFTVKGAGL VVTGTALSGE VKVGDSLWLT GVNKPMRVRA LHAQNQPTET ANAGQRIALN
IAGDAEKEQI NRGDWLLADV PPEPFTRVIV ELQTHTPLTQ WQPLHIHHAA SHVTGRVSLL
EDNLAELVFD TPLWLADNDR LVLRDISARN TLAGARVVML NPPRRGKRKP EYLQWLASLA
RAQSDADALS VHLERGAVNL ADFAWARQLN GEGMRELLQQ PGYIQAGYSL LNAPVAARWQ
RKILDTLATY HEQHRDEPGP GRERLRRMAL PMEDEALVLL LIEKMRESGD IHSHHGWLHL
PDHKAGFSEE QQAIWQKAEP LFGDEPWWVR DLAKETGTDE QAMRLTLRQA AQQGIITAIV
KDRYYRNDRI VEFANMIRDL DQECGSTCAA DFRDRLGVGR KLAIQILEYF DRIGFTRRRG
NDHLLRDALL FPEK
