ID   IF2_CITK8               Reviewed;         894 AA.
AC   A8AQ58;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=CKO_04569;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) 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; CP000822; ABV15622.1; -; Genomic_DNA.
DR   RefSeq; WP_012135301.1; NC_009792.1.
DR   AlphaFoldDB; A8AQ58; -.
DR   SMR; A8AQ58; -.
DR   STRING; 290338.CKO_04569; -.
DR   GeneID; 45138112; -.
DR   KEGG; cko:CKO_04569; -.
DR   HOGENOM; CLU_006301_6_3_6; -.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000008148; 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: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; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 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; IPR009061; DNA-bd_dom_put_sf.
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; 2.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 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..894
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008227"
FT   DOMAIN          393..562
FT                   /note="tr-type G"
FT   REGION          47..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..409
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          427..431
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          448..451
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          502..505
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          538..540
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        47..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         402..409
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         448..452
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         502..505
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   894 AA;  97560 MW;  9AE09ED9309727E5 CRC64;
     MTDVTVKALA AEIQTSVDRL VQQFADAGIP KSADDSVSAQ EKQTLLAHLN RENGSGPDKL
     TLQRKTRSTL NIPGTGGKSK SVQIEVRKKR TFVKRDPQET ERLAAEEQAQ REAEEQARRE
     AEETAKREAQ QKADREAAEQ AKRDAAEKAK REAAEKDKVS NQQTDDMTKT AQAEKARREN
     EAAELKRKAE EEARRKLEEE ARRVAEEARR MAEENKWTDN AEPTEDTSDY HVTTSQHARQ
     AEDENDREVE GGRGRSRNAK AARPAKKGNK HSESKADREE ARAAVRGGKG GKNRKGSALQ
     QSFQKPVQAV NRDVVIGETI TVGELANKMA VKGSQVIKAM MKLGAMATIN QVIDQETAQL
     VAEEMGHKVI LRRENELEEA VMSDRDTGAA AEPRAPVVTI MGHVDHGKTS LLDYIRSTKV
     ASGEAGGITQ HIGAYHVETD NGMITFLDTP GHAAFTSMRA RGAQATDIVV LVVAADDGVM
     PQTIEAIQHA KAAGVPVVVA VNKIDKPEAD PDRVKNELSQ YGILPEEWGG ESQFVHVSAK
     AGTGIDELLD AILLQAEVLE LKAVRKGMAS GAVIESFLDK GRGPVATVLV REGTLNKGDI
     VLCGFEYGRV RAMRNELGQE VLEAGPSIPV EILGLSGVPA AGDEVTVVRD EKKAREVALY
     RQGKFREVKL ARQQKSKLEN MFANMTEGEV HEVNIVLKAD VQGSVEAISD SLLKLSTDEV
     KVKIIGSGVG GITETDATLA AASNAILVGF NVRADASARK VIEAESLDLR YYSVIYNLID
     EVKAAMSGML SPELKQQIIG LAEVRDVFKS PKFGAVAGCM VTEGTIKRHN PIRVLRDNVV
     IYEGELESLR RFKDDVNEVR NGMECGIGVK NYNDVRVGDM IEVFEIIEIQ RTIA
//