ID   IF2_SHIFL               Reviewed;         882 AA.
AC   Q83JF9;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 127.
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=SF3209, S3426;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44676.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18490.1; -; Genomic_DNA.
DR   RefSeq; NP_708969.1; NC_004337.2.
DR   RefSeq; WP_000133055.1; NZ_WPGW01000004.1.
DR   AlphaFoldDB; Q83JF9; -.
DR   SMR; Q83JF9; -.
DR   STRING; 198214.SF3209; -.
DR   PRIDE; Q83JF9; -.
DR   EnsemblBacteria; AAN44676; AAN44676; SF3209.
DR   EnsemblBacteria; AAP18490; AAP18490; S3426.
DR   GeneID; 1027145; -.
DR   GeneID; 58388227; -.
DR   KEGG; sfl:SF3209; -.
DR   KEGG; sfx:S3426; -.
DR   PATRIC; fig|198214.7.peg.3809; -.
DR   HOGENOM; CLU_006301_6_3_6; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; 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; 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   Acetylation; Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..882
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137247"
FT   DOMAIN          381..550
FT                   /note="tr-type G"
FT   REGION          28..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..397
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          415..419
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          436..439
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          490..493
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          526..528
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        38..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         390..397
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         436..440
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         490..493
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   MOD_RES         800
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   882 AA;  96408 MW;  38212AE37AD88E18 CRC64;
     MTDVTIKTLA AERQTSVERL VQQFADAGIR KSADDSVSAQ EKQTLIDHLN QKNSGPDKLT
     LQRKTRSTLN IPGTGGKSKS VQIEVRKKRT FVKRDPQEAE RLAAEEQARR EAEESAKREA
     QQKAEREAAE QAKREAAEQA KREAAEKDKV SNQQDDMTKN AQAEKARREQ EAAELKRKAE
     EEARRKLEEE ARRVAEEARR MAEENKWTDN AEPTEDSSDY HVTTSQHARQ AEDESDREVE
     GGRGRGRNAK AARPKKGNKH AESKADREEA RAAVRGGKGG KRKGSSLQQG FQKPAQAVNR
     DVVIGETITV GELANKMAVK GSQVIKAMMK LGAMATINQV IDQETAQLVA EEMGHKVILR
     RENELEEAVM SDRDTGAAAE PRAPVVTIMG HVDHGKTSLL DYIRSTKVAS GEAGGITQHI
     GAYHVETENG MITFLDTPGH AAFTSMRARG AQATDIVVLV VAADDGVMPQ TIEAIQHAKA
     AQVPVVVAVN KIDKPEADPD RVKNELSQYG ILPEEWGGES QFVHVSAKAG TGIDELLDAI
     LLQAEVLELK AVRKGMASGA VIESFLDKGR GPVATVLVRE GTLHKGDIVL CGFEYGRVRA
     MRNELGQEVL EAGPSIPVEI LGLSGVPAAG DEVTVVRDEK KAREVALYRQ GKFREVKLAR
     QQKSKLENMF ANMTEGEVHE VNIVLKADVQ GSVEAISDSL LKLSTDEVKV KIIGSGVGGI
     TETDATLAAA SNAILVGFNV RADASARKVI EAESLDLRYY SVIYNLIDEV KAAMSGMLSP
     ELKQQIIGLA EVRDVFKSPK FGAIAGCMVT EGVVKRHNPI RVLRDNVVIY EGELESLRRF
     KDDVNEVRNG MECGIGVKNY NDVRTGDVIE VFEIIEIQRT IA