ID   IF2_RHILO               Reviewed;         860 AA.
AC   Q98BI8;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=mlr5554;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB51984.1; -; Genomic_DNA.
DR   RefSeq; WP_010913322.1; NC_002678.2.
DR   AlphaFoldDB; Q98BI8; -.
DR   SMR; Q98BI8; -.
DR   STRING; 266835.14025383; -.
DR   EnsemblBacteria; BAB51984; BAB51984; BAB51984.
DR   KEGG; mlo:mlr5554; -.
DR   PATRIC; fig|266835.9.peg.4416; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_0_5; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000000552; 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; 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; 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.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..860
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137240"
FT   DOMAIN          358..525
FT                   /note="tr-type G"
FT   REGION          1..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..374
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          392..396
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          413..416
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          467..470
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          503..505
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        28..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..76
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..206
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         367..374
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         413..417
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         467..470
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   860 AA;  93871 MW;  DACD54AD41E3E597 CRC64;
     MSDTKSGDDK TLSVTPMKTL TLKRPGMEQG TVRQNFSHGR TKSVVVETKK RKFSLPGDKP
     EPAAAAPVPV FTPKPPVAAA PVVQEAPKAA PPPPPRAPVE RSGMVLNELS RSEMEARRRA
     LEGSKVREVE DRQRAAEEAK RRAEDEERRK REREESARRQ AEEEARLQAE AESRRRAEEE
     ARRRAPLAAE LATADEEEEV KPKRAGAGAP VRRLVTPEVA RPAKPTKGEE DRRRGKLTLN
     SALSDEDARA RSLSSMRRRQ EKFKRAMHNE PREKVMREVI LPETITIQEL AQRMSERAVD
     VVKFFMKQGQ ILKPGDVIDA DTAELVATEF GHTVRRVAES DIEEGLFNIA DNAEDLVPRP
     PVVTIMGHVD HGKTSLLDAI RNANVVSGEA GGITQHIGAY QVEKNGQKIT FIDTPGHAAF
     TAMRARGAQA TDIAILVVAA DDSVMPQTIE SISHAKAAGV PIIVAINKID KHDADPQKVR
     SELLRHEVFV ESMGGEVLDV EVSATKGTNL DKLLEAILLQ AEILDLKANP DRTAEGVVIE
     AQLDKGRGPV ATVLVQTGTL MPGDILVAGN EWGRVRALVN DRGEQIKEAP PAMPVEVLGL
     QGTPLAGDRF AVVNNEARAR EITEYRQRLA REKAVAKHAG QRGSLEQMMS QLQTSGLKEF
     PLVIKGDVQG SIEAINAALD KLGTDEVRAR IVHAGAGAIT ESDVSLAETS GAAIIGFNVR
     ANVQARAAAA AAGIEIRYYS IIYNLVDDVK AALSGLLSPE RRETFIGNAE ILEIFDITKV
     GKIAGCRVTE GKVERGAGVR LIRDNVVIHE GTLKTLKRFK DEVSEVPGGQ ECGMAFQNYE
     DMRVGDIIEC FRVEMVTRTL