IF2_AERHH
ID IF2_AERHH Reviewed; 897 AA.
AC A0KNE3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=AHA_3303;
OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=380703;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC 2358 / NCIMB 9240 / NCTC 8049;
RX PubMed=16980456; DOI=10.1128/jb.00621-06;
RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL J. Bacteriol. 188:8272-8282(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; CP000462; ABK38444.1; -; Genomic_DNA.
DR RefSeq; WP_011707074.1; NC_008570.1.
DR RefSeq; YP_857794.1; NC_008570.1.
DR AlphaFoldDB; A0KNE3; -.
DR SMR; A0KNE3; -.
DR STRING; 380703.AHA_3303; -.
DR PRIDE; A0KNE3; -.
DR EnsemblBacteria; ABK38444; ABK38444; AHA_3303.
DR KEGG; aha:AHA_3303; -.
DR PATRIC; fig|380703.7.peg.3299; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000756; 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 Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..897
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008191"
FT DOMAIN 397..566
FT /note="tr-type G"
FT REGION 69..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..413
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 431..435
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 452..455
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 506..509
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 542..544
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 69..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 406..413
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 452..456
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 506..509
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 897 AA; 98170 MW; 3EB1C3654486C3FE CRC64;
MAEVSVKQLA TDIDTPVDRL LQQFVDAGIS KSKADDMVSE SEKQTLLAHL KKQHGGDEVA
APARMTLQRK TKSTISVQGT GGKNKEVQVE VRKSRTYVRR SALEDEQRQA EAEETARLEA
EEKARREAEE KARLDAEEKA RREAEQARRE AEEKARIEAQ QKARQAQQPA KAAGSTAQQE
AEKMAKREAE ELKRQQEQAA LTKAEELAAK KAEEARVMAE QNAARWAEEE AARAKESSDY
HLTTNKHAQA AEDELDRKEE TSRRTAAAAK GPKKAGRRED DRDARNPRAR KGKRGKVATP
NAMKHGFNKP AAAVNRDVVI GETITVAELA NKMAVKGVEV IKVMMKMGAM ATINQVIDQE
TAQLVAEEMG HKVVLRRENE LEEAVLSDRD ETSEAKPRAP VVTIMGHVDH GKTSLLDYIR
KAKVAAGEAG GITQHIGAYH VETDSGMITF LDTPGHAAFT SMRARGAKAT DIVVLVVAAD
DGVMPQTIEA IQHAKAAEVP LVVAVNKIDK PEADPDRVKT ELARYNVMSE DWGGDCQFVH
VSAKSGQGID DLLEAILIQS EVLELKAVVD GMANGVVIES FLDKGRGPVA TVLVQEGTLR
QGDIVLCGLE YGRVRAMRDE LGREIKEAGP SLPVEILGLS GVPSAGDEAT VVRDEKKARE
VALYRQGKFR EVKLARQQKA KLENMFANMT EGEVSEVNVV IKADVQGSVE AICDALVKLS
TDEVKVKIVG SGVGGITETD ATLAAASSAI LVGFNVRADA SARKVIEAES LDLRYYSVIY
DLIDEVKQAM SGMLAPEYRQ EIIGLAEVRS VFKSPKFGAV AGCMVTEGVV KRSNRIRVLR
DNVVIYEGEL ESLRRFKDDV NEVKNGYECG IAVKNYNDVR EGDQIEVYET VEIQRTL
