IF2_VARPS
ID IF2_VARPS Reviewed; 984 AA.
AC C5CLW3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Vapar_2748;
OS Variovorax paradoxus (strain S110).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=543728;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S110;
RX PubMed=21183664; DOI=10.1128/jb.00925-10;
RA Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G.,
RA O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C.,
RA Ovchinnikova G., Goodwin L., Han C.;
RT "Complete genome sequence of the metabolically versatile plant growth-
RT promoting endophyte, Variovorax paradoxus S110.";
RL J. Bacteriol. 193:1183-1190(2011).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; CP001635; ACS19370.1; -; Genomic_DNA.
DR RefSeq; WP_012747852.1; NC_012791.1.
DR AlphaFoldDB; C5CLW3; -.
DR SMR; C5CLW3; -.
DR STRING; 543728.Vapar_2748; -.
DR PRIDE; C5CLW3; -.
DR EnsemblBacteria; ACS19370; ACS19370; Vapar_2748.
DR GeneID; 45057016; -.
DR KEGG; vap:Vapar_2748; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_2_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF46955; SSF46955; 1.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..984
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202788"
FT DOMAIN 484..653
FT /note="tr-type G"
FT REGION 92..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..500
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 518..522
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 539..542
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 593..596
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 629..631
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 126..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 493..500
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 539..543
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 593..596
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 984 AA; 104803 MW; 3D98ADADA65BD0B9 CRC64;
MSSTTVAEFA NELKKTPETL LDQLKSAGVP KAAPTDALTE ADKQRLLGFL KASHGTAEPE
RKKITLTKKS TSEIKQADAT GRARTIQVEV RKKRTFIQRD DGHPATPEVQ PVAEAPAAAP
AAPRIDEAEL ARREEEARRQ AELIRRQEEE LAEKRRLREE AEAREREQAE KAERAEQAEQ
EAARIAAEKK AADAAAAAPA KEAAKPAAAP VAAAAAAAEQ QAADTKLAAQ TAATQAKEDA
KAKAAAESKA RADEEAARAK DLDERRRKAL AEAEAIRAMM NAPARVLVPH KAPEKPQPEK
AAVKGTLHKP AAPAARPGAP AAPGAAAAPG AAGAGKEVKS AKLSSSWAGD PAKKKEIKTR
GDASGGVGRG NWRGGPRGRR GSNDRGGHEE HVQAAPVEAR ILEVHVPETI TVAELAHKMA
VKAQEVIKQL MKLGQMATIN QSLDQDTAMI LVEEMGHNAV VAALDDPEAF TDEDVSAQTA
EALPRAPVVT VMGHVDHGKT SLLDYIRRAK VAAGEAGGIT QHIGAYHVQT ERGMVSFLDT
PGHEAFTAMR ARGAQATDIV ILVVAADDGV MPQTKEAIKH AKAAGVPIVV AINKIDKPDA
SPDRVKQELV AEEVVPEEYG GDVPFVPVSA KTGQGIDDLL EQVLLQAEVL ELKAPVDAAA
KGLVIEAQLD KGRGPVATVL VQSGTLKTGD VVLAGSTYGR VRAMLDEDGR TIKSAGPSIP
VEIQGLTEVP QAGDEFMVMS DERRAREIAT YRAGKFRNTK LAKAQAANLQ NMFTDLSAGE
VQTLRIIIKA DVQGSQEALA QSLLKLATDE VKVQIVYAGV GGISESDINL AIASKAIVIG
FNVRADAGAR KLAEGNGVQL NYYSIIYDAV DEIKVAMSGM LAPERREEII GSAEIRTVFV
ASKIGTVAGS YITSGSVNRS AHFRLLRDNV VIYTGEVDSI KRMKDDVREV REGFECGIKL
KNYNDIKEGD QLEFFEIKEI ARTL
