IF2_CITK8
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 03-AUG-2022, entry version 89.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CKO_04569;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; 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 EnsemblBacteria; ABV15622; ABV15622; CKO_04569.
DR GeneID; 45138112; -.
DR KEGG; cko:CKO_04569; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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: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; 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 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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF46955; SSF46955; 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; 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