IF2_HAEIE
ID IF2_HAEIE Reviewed; 836 AA.
AC A5UBT6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=CGSHiEE_04160;
OS Haemophilus influenzae (strain PittEE).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374930;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittEE;
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
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; CP000671; ABQ98237.1; -; Genomic_DNA.
DR RefSeq; WP_011961910.1; NC_009566.1.
DR AlphaFoldDB; A5UBT6; -.
DR SMR; A5UBT6; -.
DR KEGG; hip:CGSHiEE_04160; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
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; 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; 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.
FT CHAIN 1..836
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335475"
FT DOMAIN 335..505
FT /note="tr-type G"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..351
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 369..373
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 391..394
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 445..448
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 481..483
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 14..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 344..351
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 391..395
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 445..448
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 836 AA; 91631 MW; 5BA4DCDB109A86E1 CRC64;
MLRLMRQKKL SIQRRTKTTV SSTTTGGKSK EVQVEVRKKR TVKTDIAQQE EAKLKAQQEA
EAKKIAEQKA IEEKARLEAE KVAAKKEADE KVKAETAKPV KSAVDSKVKS VDPEKEKRKA
EEAELRRKAE ELARQKAEEQ ARRAAEEAKR YAEADDSDNE SSSEDYSDYN LSSRYALEAE
DEEDRRNENR GRGKNKVAKA KKGGRDDENS KNSKNERESN RKNQKDAKFG KGKNGKKGAA
LQQAFTKPAQ VVKSDVVIGE TITVAELANK MAVKATEIIK MMMKMGEMVT INQVIDQETA
QLVAEELGHK VILRNENELE EAVLGDRDVN AEKVTRAPVV TIMGHVDHGK TSLLDYIRKA
KVAAGEAGGI TQHIGAYHVE MDDGKMITFL DTPGHAAFTS MRARGAKATD IVVLVVAADD
GVMPQTIEAI QHAKAAGAPL VVAVNKIDKP EANLDRVEQE LLQHDVISEK FGGDVQFVPV
SAKKGTGVDD LLDAILLQSE VLELTAVKDG MASGVVIESY LDKGRGPVAT ILVQSGTLRK
GDIVLCGFEY GRVRAMRDEN GKEVDEAGPS IPVELLGLSG VPAAGDEATV VRDEKKAREV
ALYRQGKFRE VKLARQQKAK LENMFSNMSE GDVAELNVIV KADVQGSVEA IVQALNELST
NEVKVKVVGS GVGGITETDA TLATASNAII VGFNVRADAT ARRVIEAENI DLRYYSIIYE
LLNEIKAAMS GMLEPEFKQE IIGLAEVRDV FRHPKFGAIA GCMVTEGVVK RNNPIRVLRD
NVVIFEGELE SLRRFKDDVS EVRNGMECGI GVKNYNDVKV GDQIEVFEVV EVKRSI
