IF2_ACTP2
ID IF2_ACTP2 Reviewed; 841 AA.
AC A3N005;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=APL_0639;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN73741.1; -; Genomic_DNA.
DR RefSeq; WP_005600786.1; NC_009053.1.
DR AlphaFoldDB; A3N005; -.
DR SMR; A3N005; -.
DR STRING; 416269.APL_0639; -.
DR PRIDE; A3N005; -.
DR EnsemblBacteria; ABN73741; ABN73741; APL_0639.
DR KEGG; apl:APL_0639; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001432; 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; 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; 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; Reference proteome.
FT CHAIN 1..841
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008190"
FT DOMAIN 340..510
FT /note="tr-type G"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..356
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 374..378
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 396..399
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 450..453
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 486..488
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 349..356
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 396..400
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 450..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 841 AA; 91495 MW; AE552E82ED6B133E CRC64;
MSDNEIKNEA PKKLSLQRRT KTTVADGKVQ VEVRKSRKID TAAVKKAQEE AALKAKQEAE
AKAQAEKTAA EQAKAEAEAA KKAEGAKVEA TKKSAPAVPV MPNSKPKAAA PKAEQPKQEK
ALDPEKEAKK KEEAELRRKQ EELARQKAEM EAKRAAENAR RLAEIAREEA AENGEEFEDD
RFTSSYAREA DRDNDRRSEA NRGRGKGGVN KAKKGDREDK NERNADRRNQ KDVKGKGKNA
KKGSALQQAF TKPVQVNKAD VVIGETITVA ELANKMAVKA TEIIKTMMKM GEMVTINQVI
DQETAQLVAE EMGHKVILRN ENELEDAVME DRDVDAEKVT RAPVVTIMGH VDHGKTSLLD
YIRKAKVAAG EAGGITQHIG AYHVETEDGK MITFLDTPGH AAFTSMRARG AKATDIVVLV
VAADDGVMPQ TIEAIQHARA AGAPIVVAVN KIDKPEANPD RVEQELLQHE VVSEKFGGDV
QFVPVSAKKG LGIDDLLEAI LLQSEVLELT AVKEGMASGV VIESYLDKGR GPVATILVQS
GTLNKGDIVL CGFEYGRVRA MRDENGKEVD SAGPSIPVEV LGLSGVPAAG DEATVVRDEK
KAREVALFRQ GKFREVKLAR QQKAKLENMF SNMTAGDVAE LNVIVKADVQ GSVEAICQSL
AELSTDEVKV KVVGSGVGGI TETDATLAAA SNAIMVGFNV RADASARRVI EAENIDLRYY
SIIYELLNEI KAAMSGMLQP EFKQEIIGLA EVRDVFRHPK FGAIAGCMVT EGVVKRNNPI
RVLRDNVVIF EGELESLRRF KDDVSEVRNG MECGIGVKNY NDVKVGDQIE VFEVVEVKRS
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