ID   IF2_PARDP               Reviewed;         848 AA.
AC   A1B587;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=Pden_2594;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
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   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000489; ABL70681.1; -; Genomic_DNA.
DR   RefSeq; WP_011748874.1; NC_008686.1.
DR   AlphaFoldDB; A1B587; -.
DR   SMR; A1B587; -.
DR   STRING; 318586.Pden_2594; -.
DR   EnsemblBacteria; ABL70681; ABL70681; Pden_2594.
DR   GeneID; 75502056; -.
DR   KEGG; pde:Pden_2594; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_10_1_5; -.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000000361; Chromosome 1.
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; Reference proteome.
FT   CHAIN           1..848
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008293"
FT   DOMAIN          346..514
FT                   /note="tr-type G"
FT   REGION          1..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..362
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          380..384
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          402..405
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          456..459
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          492..494
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        72..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         355..362
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         402..406
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         456..459
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   848 AA;  91294 MW;  B7DB50802DADE02D CRC64;
     MSDTDGKKPL GLGGGRSGHV KQSFSHGRTH NVVVETKRKR VVVPGKTGAA AGGGRSGSPS
     AVSGDPSKRP AGISDAEMER RMAALRAAKA REVEEAAQRI ADEKAREEER ERRRLELEAK
     EREEREREEA LRLKAEEDER RAREAELREK KKAEIAKPKT EARPATPADR AAAEAAAVRA
     ETKGVSAAGP RKTDRDRDTR GGGGDDRDSR NKGRDDSRRT GKLSLSQALD GEGGRQRSLA
     AMKRKQEKAR QKAMGGNQRA EKQVRDVQLP ETIVVSELAN RMAERTPDVI KSLMRMGMMV
     TANQSIDADT AELVIDEFGH HAVRVSDADV EQVIDQVEDK PEDLQPRAPI ITIMGHVDHG
     KTSLLDAIRH ANVVAGEAGG ITQHIGAYQV KASNGAVLTF LDTPGHAAFT SMRARGAQVT
     DIVVLVVAAD DAVMPQTVEA INHAKAAKVP MIVAINKIDK PAANPQKVRT DLLLHEVVVE
     AMSGEVQDVE VSAKTGQGLD TLLEAIALQA EILELKANPD RPAQGAVIEA QLDVGRGPVA
     TVLVQNGTLK RGDIFVVGEQ WGKVRALIND KGERVDEAGP SVPVEVLGLN GTPEAGDVLN
     VVSTEAQARE IADYRIQAAK DKRAAAGAAI TLDQMLAKAK ADENVAELPV VIKADVQGSA
     EAIVQALEKI GNDEVRVRVL HYGVGAITES DIGLAEASQA PVIGFNVRAN APARNAANQK
     GVEIRYYSII YDLVDDIKAA ASGLLSAEVR ENFIGYAEIK EVFRVSGVGN VAGCLVTEGV
     ARRSAGVRLL RDNVVIHEGT LKTLKRFKDE VKEVQSGQEC GMAFENYDDI RKGDVIEIFE
     REEVQRQL
//