IF2_SHIF8
ID IF2_SHIF8 Reviewed; 882 AA.
AC Q0T0B3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SFV_3198;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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; CP000266; ABF05252.1; -; Genomic_DNA.
DR RefSeq; WP_000133056.1; NC_008258.1.
DR AlphaFoldDB; Q0T0B3; -.
DR SMR; Q0T0B3; -.
DR EnsemblBacteria; ABF05252; ABF05252; SFV_3198.
DR KEGG; sfv:SFV_3198; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR BioCyc; SFLE373384:SFV_RS17660-MON; -.
DR Proteomes; UP000000659; 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.
FT CHAIN 1..882
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008338"
FT DOMAIN 381..550
FT /note="tr-type G"
FT REGION 28..294
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; 96436 MW; 017653A9628AC407 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 FQKPAQVVNR
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
