ID IF2_RHOPB Reviewed; 880 AA.
AC Q21C31;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RPC_0480;
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-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; CP000301; ABD86055.1; -; Genomic_DNA.
DR AlphaFoldDB; Q21C31; -.
DR SMR; Q21C31; -.
DR STRING; 316056.RPC_0480; -.
DR KEGG; rpc:RPC_0480; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OrthoDB; 9811804at2; -.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR004161; EFTu-like_2.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..880
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008316"
FT DOMAIN 376..547
FT /note="tr-type G"
FT REGION 1..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..392
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 410..414
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 433..436
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 487..490
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 523..525
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 8..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 385..392
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 433..437
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 487..490
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 880 AA; 94258 MW; 804E0D6DF50ABC24 CRC64;
MVDTKNPGDK TLSVSPSKTL TLKRGVEQGT VRQSFSHGRT KQVVVEKRGK RRVGGDGPAD
APAAPAPVAA AKPAPVRAPM SRPPQSSHRG GGSGVVLRTL TEDERTARAS ALADARIRDE
EERKAAEAEL ARRNSKEGIE QAEREAAEAR KKAEEERHRQ DEEAKRKAEL EAKKRFGEEE
AKKAAAAAPA KTTAATTATA AKPGAPARAP GVAADATDED EGPRQIRRGP GGAARPVVAP
KPTAKPAPAK QRGRLTLVTA LSADDVRERS IASFRRRTQR LKGHQSNEPK EKLVREVIIP
EAITIQELAN RMAERAVDVI RMLMKQGQMV KITDVIDADT AQLIAEELGH SVKRVAASDV
EEGLFDIVDD ATDTEPRSPV VTVMGHVDHG KTSLLDALRH ANVVSGEAGG ITQHIGAYQV
TSPESGKKIT FIDTPGHAAF TAMRARGAKV TDIVVLVVAA DDGVMPQTIE AINHAKAAKV
PVIVAINKID KQDAKPERVR TELLQYGIQV ESLGGDVVDV EVSAKNKTNL DKLLEMIALQ
AELLDLKTNT ERPAEGTVIE AKLDRGRGPV ATVLVQRGTL RVGDIIVAGA EMGRVRALIS
DQGVTLTEAG PSVPVEVLGF NGPPEAGDRM AVVDSEARAR QVTSYRAHQK REKSASAVSG
LRGSLEQMMS QLKTTGRKDF PLIIKADVAG SLEAILGSLE KLGTDEVTAR ILHAGVGGIS
ESDVTLAEGF NAAIIGFNVR AHKEAAAAAK RNGIEIRYYN IIYDLVDDVK KAMSGLLAPT
LRETMLGNAL ILEVFNISKV GKVAGCRVTD GSVERGANVR LIRDNVVVHE GKLSTLKRFK
DEVKEVQSGQ ECGMAFENYG DMRAGDIIEC YRVETIQRSL
//
