IF2_VEREI
ID IF2_VEREI Reviewed; 990 AA.
AC A1WLI3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Veis_2749;
OS Verminephrobacter eiseniae (strain EF01-2).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Verminephrobacter.
OX NCBI_TaxID=391735;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF01-2;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000542; ABM58490.1; -; Genomic_DNA.
DR RefSeq; WP_011810488.1; NC_008786.1.
DR AlphaFoldDB; A1WLI3; -.
DR SMR; A1WLI3; -.
DR STRING; 391735.Veis_2749; -.
DR PRIDE; A1WLI3; -.
DR EnsemblBacteria; ABM58490; ABM58490; Veis_2749.
DR KEGG; vei:Veis_2749; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; RDVMMAG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000374; 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: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; Reference proteome.
FT CHAIN 1..990
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335518"
FT DOMAIN 490..659
FT /note="tr-type G"
FT REGION 92..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..506
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 524..528
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 545..548
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 599..602
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 635..637
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 156..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 499..506
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 545..549
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 599..602
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 990 AA; 105143 MW; 4FBB4B708A35CF69 CRC64;
MSSNTVAEFA TELKKSPATL LDQLKAAGVG KAALSDALTE SDKQRLLAYL QASHGTTSVD
RKKITLVKKS TSEIKQADAT GKARTIQVEV RKKRTFVKRD DAQEGAADGA GSAAFAEPEH
PAPAAQHDVP EAPAEQAQAD AAPAADGAAP ALSSEDQELA RREEQARHQA ELIRRQEAEL
AAKRAAREAR EKREREAEER AAAYAAQEAE KKAAASAVKQ VATREQAAEA TARNAAQLQA
RAKAAAESKA RSDEEAARAA DLDARRRKAE AEAAAIRSML ATPKKAVMVA KKPEPPPKPV
PKPAAAAGDA KKGTLHKPAV GATRTAAGAA RAGAAAGAPG AGKEVKSAKL SSSWAGDPAK
KKEIKTRGDS SGGVGRNNWR GGPRGRRGDS RDQRDEHLQA APAETRIIEV HVPETITVAE
VAHKMSIKAS EVIKALMKMG QMVTINQPLD QDTAMIVVEE LGHKAVVAAL DDPEAFADDD
VAQQSIEVLP RAPVVTVMGH VDHGKTSLLD YIRRAKVAAS EAGGITQHIG AYHVQTPRGM
VSFLDTPGHE AFTAMRARGA QATDIVILVV AADDGVMPQT REAIKHAKAA GVPIVVAITK
ADKPDANLDR VKQELIGEQV VPEDYGGDSP FVAVSSKTGQ GIDALLEHVL LQADVMELKA
PVDALAKGLV IEAQLDKGRG PVATVLVQSG TLKVGDVVLA GQTFGRVRAM LDENGRPAKT
AGPSIPVEIQ GLTEVPQAGD EFMVLTDERR AREIATYRAG RFRNTKLAKQ QAAKLEHVFA
DMTAGEVKML PIIVKADVQG SQEALAQSLL KLSTDEVKVQ LVYAAVGAIS ESDINLAIAS
KAVVIGFNVR ADAGARKLAE GNGVALHYYS IIYDAVDELR VAMSGMLAPE QREEIIGTAE
IRTVFTASKI GTVAGSYITS GMVHRNARFR LLRANVVVHT GEVDSIKRLK DDVREVKEGF
ECGIKLKNYS DILEGDQLEF FDIKQIARTL
