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Protein

Selenocysteine-specific elongation factor

Gene

selB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 148GTPBy similarity
Nucleotide bindingi57 – 615GTPBy similarity
Nucleotide bindingi112 – 1154GTPBy similarity

GO - Molecular functioni

  • GDP binding Source: EcoCyc
  • GTPase activity Source: EcoCyc
  • GTP binding Source: EcoCyc
  • selenocysteine insertion sequence binding Source: EcoCyc
  • translation elongation factor activity Source: InterPro
  • tRNA binding Source: EcoCyc

GO - Biological processi

  • selenocysteine incorporation Source: EcoCyc
  • selenocysteine metabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10942-MONOMER.
ECOL316407:JW3563-MONOMER.
MetaCyc:EG10942-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Selenocysteine-specific elongation factor
Alternative name(s):
SelB translation factor
Gene namesi
Name:selB
Synonyms:fdhA
Ordered Locus Names:b3590, JW3563
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10942. selB.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 614614Selenocysteine-specific elongation factorPRO_0000091474Add
BLAST

Proteomic databases

PaxDbiP14081.
PRIDEiP14081.

Interactioni

Protein-protein interaction databases

BioGridi4261875. 4 interactions.
DIPiDIP-10848N.
IntActiP14081. 42 interactions.
MINTiMINT-1221874.
STRINGi511145.b3590.

Structurei

Secondary structure

1
614
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi489 – 49810Combined sources
Helixi499 – 5013Combined sources
Beta strandi503 – 5053Combined sources
Helixi509 – 5157Combined sources
Helixi520 – 53213Combined sources
Beta strandi535 – 5406Combined sources
Beta strandi543 – 5464Combined sources
Helixi547 – 56418Combined sources
Beta strandi565 – 5684Combined sources
Helixi569 – 5768Combined sources
Helixi580 – 59213Combined sources
Beta strandi595 – 5995Combined sources
Beta strandi602 – 6054Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PJPX-ray2.30A487-607[»]
ProteinModelPortaliP14081.
SMRiP14081. Positions 2-325, 419-607.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14081.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 173173tr-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 148G1PROSITE-ProRule annotation
Regioni35 – 395G2PROSITE-ProRule annotation
Regioni57 – 604G3PROSITE-ProRule annotation
Regioni112 – 1154G4PROSITE-ProRule annotation
Regioni147 – 1493G5PROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. SelB subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105EM7. Bacteria.
COG3276. LUCA.
HOGENOMiHOG000163837.
InParanoidiP14081.
KOiK03833.
OMAiYAIDRVF.
OrthoDBiEOG6V1M2Q.
PhylomeDBiP14081.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR015190. Elong_fac_SelB-wing-hlx_typ-2.
IPR015191. Elong_fac_SelB-wing-hlx_typ-3.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004535. Transl_elong_SelB.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF09106. SelB-wing_2. 1 hit.
PF09107. SelB-wing_3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF46785. SSF46785. 3 hits.
SSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00475. selB. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14081-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIIATAGHVD HGKTTLLQAI TGVNADRLPE EKKRGMTIDL GYAYWPQPDG
60 70 80 90 100
RVPGFIDVPG HEKFLSNMLA GVGGIDHALL VVACDDGVMA QTREHLAILQ
110 120 130 140 150
LTGNPMLTVA LTKADRVDEA RVDEVERQVK EVLREYGFAE AKLFITAATE
160 170 180 190 200
GRGMDALREH LLQLPEREHA SQHSFRLAID RAFTVKGAGL VVTGTALSGE
210 220 230 240 250
VKVGDSLWLT GVNKPMRVRA LHAQNQPTET ANAGQRIALN IAGDAEKEQI
260 270 280 290 300
NRGDWLLADV PPEPFTRVIV ELQTHTPLTQ WQPLHIHHAA SHVTGRVSLL
310 320 330 340 350
EDNLAELVFD TPLWLADNDR LVLRDISARN TLAGARVVML NPPRRGKRKP
360 370 380 390 400
EYLQWLASLA RAQSDADALS VHLERGAVNL ADFAWARQLN GEGMRELLQQ
410 420 430 440 450
PGYIQAGYSL LNAPVAARWQ RKILDTLATY HEQHRDEPGP GRERLRRMAL
460 470 480 490 500
PMEDEALVLL LIEKMRESGD IHSHHGWLHL PDHKAGFSEE QQAIWQKAEP
510 520 530 540 550
LFGDEPWWVR DLAKETGTDE QAMRLTLRQA AQQGIITAIV KDRYYRNDRI
560 570 580 590 600
VEFANMIRDL DQECGSTCAA DFRDRLGVGR KLAIQILEYF DRIGFTRRRG
610
NDHLLRDALL FPEK
Length:614
Mass (Da):68,867
Last modified:November 1, 1997 - v3
Checksum:i1C0690A2672FCB1A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16644 Genomic DNA. Translation: CAA34637.1.
U00039 Genomic DNA. Translation: AAB18567.1. Frameshift.
U00096 Genomic DNA. Translation: AAC76614.1.
AP009048 Genomic DNA. Translation: BAE77703.1.
PIRiJV0050. EFECSB.
RefSeqiNP_418047.1. NC_000913.3.
WP_000582468.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76614; AAC76614; b3590.
BAE77703; BAE77703; BAE77703.
GeneIDi948103.
KEGGiecj:JW3563.
eco:b3590.
PATRICi32122658. VBIEscCol129921_3706.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16644 Genomic DNA. Translation: CAA34637.1.
U00039 Genomic DNA. Translation: AAB18567.1. Frameshift.
U00096 Genomic DNA. Translation: AAC76614.1.
AP009048 Genomic DNA. Translation: BAE77703.1.
PIRiJV0050. EFECSB.
RefSeqiNP_418047.1. NC_000913.3.
WP_000582468.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PJPX-ray2.30A487-607[»]
ProteinModelPortaliP14081.
SMRiP14081. Positions 2-325, 419-607.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261875. 4 interactions.
DIPiDIP-10848N.
IntActiP14081. 42 interactions.
MINTiMINT-1221874.
STRINGi511145.b3590.

Proteomic databases

PaxDbiP14081.
PRIDEiP14081.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76614; AAC76614; b3590.
BAE77703; BAE77703; BAE77703.
GeneIDi948103.
KEGGiecj:JW3563.
eco:b3590.
PATRICi32122658. VBIEscCol129921_3706.

Organism-specific databases

EchoBASEiEB0935.
EcoGeneiEG10942. selB.

Phylogenomic databases

eggNOGiENOG4105EM7. Bacteria.
COG3276. LUCA.
HOGENOMiHOG000163837.
InParanoidiP14081.
KOiK03833.
OMAiYAIDRVF.
OrthoDBiEOG6V1M2Q.
PhylomeDBiP14081.

Enzyme and pathway databases

BioCyciEcoCyc:EG10942-MONOMER.
ECOL316407:JW3563-MONOMER.
MetaCyc:EG10942-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP14081.
PROiP14081.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR004161. EFTu-like_2.
IPR015190. Elong_fac_SelB-wing-hlx_typ-2.
IPR015191. Elong_fac_SelB-wing-hlx_typ-3.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004535. Transl_elong_SelB.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF09106. SelB-wing_2. 1 hit.
PF09107. SelB-wing_3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF46785. SSF46785. 3 hits.
SSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00475. selB. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein."
    Forchhammer K., Leinfelder W., Boeck A.
    Nature 342:453-456(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  2. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO C-TERMINUS.
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Purification and biochemical characterization of SELB, a translation factor involved in selenoprotein synthesis."
    Forchhammer K., Rucknagel K.-P., Bock A.
    J. Biol. Chem. 265:9346-9350(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.

Entry informationi

Entry nameiSELB_ECOLI
AccessioniPrimary (citable) accession number: P14081
Secondary accession number(s): Q2M7Q3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

There are about 1100 copies of SelB per E.coli cell.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.