ID   IF2_KORVE               Reviewed;        1011 AA.
AC   Q1IIT3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Acid345_4217;
OS   Koribacter versatilis (strain Ellin345).
OC   Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC   Candidatus Koribacter.
OX   NCBI_TaxID=204669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin345;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP000360; ABF43217.1; -; Genomic_DNA.
DR   RefSeq; WP_011525016.1; NC_008009.1.
DR   AlphaFoldDB; Q1IIT3; -.
DR   SMR; Q1IIT3; -.
DR   STRING; 204669.Acid345_4217; -.
DR   PRIDE; Q1IIT3; -.
DR   EnsemblBacteria; ABF43217; ABF43217; Acid345_4217.
DR   KEGG; aba:Acid345_4217; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_0; -.
DR   OMA; QVRPEMI; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000002432; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   PRINTS; PR00315; ELONGATNFCT.
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; Reference proteome.
FT   CHAIN           1..1011
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000335452"
FT   DOMAIN          502..678
FT                   /note="tr-type G"
FT   REGION          49..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..518
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          536..540
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          564..567
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          618..621
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          654..656
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        49..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..129
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..253
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..292
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         511..518
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         564..568
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         618..621
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1011 AA;  106830 MW;  ED87202E2A0C479C CRC64;
     MKIRINDLAR ELEVKSKAIL DALTKVGVTE KKTHSSSIED HEAVLVKKYI HEHGTEESPR
     RRSAGEDEFK PKIDLSKISK PGDVLKALTQ KAAPPPPPPP PPRPAVKAPS PVSQEPRPPA
     VPPAPQKPAV FARPASETVH TPPEPPKPRF ITPASVAAQR PVITPPKPPV PPAPPVAVAP
     PAVIEPAAPA EEPKAAAPAT TAPEAPEVKA PVSPERVAPA ADTGAHVTAK PEAPAAPGAA
     TPAPTPGRPL PGVPLRQQTP GRRMIVPQTG PRPVYSAPPP APPRPTPPPQ MSQGAGTRPG
     MPVRGQPIFQ RRPQSGPGGG SGGPGGFQRP GGPPRPGDRP RGPHPTRQFP SGPRPMGGIG
     LAPPGAPANK PAGRPAPARR PGQRYVPRGQ KEGPMKGFVP PPRLSLSNEP LPITRNITIS
     EGISVKDLAE KLGIRAKDLI ARLLARGVFA TVNQTLEASL ASEMANHFGA STDVITFEDQ
     LAQETAKAAG ETPEEAAANA VVRPPVVTIM GHVDHGKTSL LDAIRATDVA GGEAGGITQH
     IGAYKVAIGD PNSPAFGREI VFLDTPGHEA FTRMRARGSK ITDIVVIVVA ADDGVMPQTV
     EAIDHARAAN VPIIVAVNKI DKPDAMPERV KKQLADRGLM PEDWGGNTVF VDVSAKQKTN
     LNLLMEMICL VADLGDLKAN PDRMASGTVV EAKLDRGRGP VATVLVQNGT LRTSDNFVVG
     NAFGKVRAMF NDRGVSLDTA GPSTPVEIIG LETLPQAGDQ FTVVADREKA RDISEYREGR
     AREAQLAKSS RVSLEGLAEQ LKTAGQKDLP IILKGDVQGS VEVLNDLLSK MSTEKVKITM
     IRSGVGAITE SDVLLASASN AIIIGFNVRP ERKAQELAVQ EGVDIRLHSI IYELQDEMKK
     AMLGLLEPII KETYQGRADV KDTFRIPKVG TIAGCQVADG IIKRDSHVRL VRDNVVIYTG
     KIGSLKRFKD DASEVRNGME CGIGIAGYGD IRSGDVIEAF TSEKIAADSL H