IF2_ECO8A
ID IF2_ECO8A Reviewed; 890 AA.
AC B7M076;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=ECIAI1_3318;
OS Escherichia coli O8 (strain IAI1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI1;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928160; CAR00132.1; -; Genomic_DNA.
DR RefSeq; WP_000133044.1; NC_011741.1.
DR AlphaFoldDB; B7M076; -.
DR SMR; B7M076; -.
DR GeneID; 58462836; -.
DR KEGG; ecr:ECIAI1_3318; -.
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; 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..890
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000117330"
FT DOMAIN 389..558
FT /note="tr-type G"
FT REGION 45..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..405
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 423..427
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 444..447
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 498..501
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 534..536
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 45..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 398..405
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 444..448
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 498..501
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT MOD_RES 808
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 890 AA; 97350 MW; 86B9F9B2AE773DDE CRC64;
MTDVTIKTLA AERQTSVERL VQQFADAGIR KSADDSVSAQ EKQTLIDHLN QKNSGPDKLT
LQRKTRSTLN IPGTGGKSKS VQIEVRKKRT FVKRDPQEAE RLAAEEQAQR EAEEQARREA
EESAKREAQQ KAEREAAEQA KREAAEQAKR EAAEKDKVSN QQDDMTKNAQ AEKARREQEA
AELKRKAEEE ARRKLEEEAR RVAEEARRMA EENKWTDNAE PTEDSSDYHV TTSQHARQAE
DESDREVEGG RGRGRNAKAA RPKKGNKHAE SKADREEARA AVRGGKGGKR KGSSLQQGFQ
KPAQAVNRDV VIGETITVGE LANKMAVKGS QVIKAMMKLG AMATINQVID QETAQLVAEE
MGHKVILRRE NELEEAVMSD RDTGAAAEPR APVVTIMGHV DHGKTSLLDY IRSTKVASGE
AGGITQHIGA YHVETENGMI TFLDTPGHAA FTSMRARGAQ ATDIVVLVVA ADDGVMPQTI
EAIQHAKAAQ VPVVVAVNKI DKPEADPDRV KNELSQYGIL PEEWGGESQF VHVSAKAGTG
IDELLDAILL QAEVLELKAV RKGMASGAVI ESFLDKGRGP VATVLVREGT LHKGDIVLCG
FEYGRVRAMR NELGQEVLEA GPSIPVEILG LSGVPAAGDE VTVVRDEKKA REVALYRQGK
FREVKLARQQ KSKLENMFAN MTEGEVHEVN IVLKADVQGS VEAISDSLLK LSTDEVKVKI
IGSGVGGITE TDATLAAASN AILVGFNVRA DASARKVIEA ESLDLRYYSV IYNLIDEVKA
AMSGMLSPEL KQQIIGLAEV RDVFKSPKFG AIAGCMVTEG VVKRHNPIRV LRDNVVIYEG
ELESLRRFKD DVNEVRNGME CGIGVKNYND VRTGDVIEVF EIIEIQRTIA
