IF2_HISS2
ID IF2_HISS2 Reviewed; 831 AA.
AC B0UU13;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=HSM_1290;
OS Histophilus somni (strain 2336) (Haemophilus somnus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=228400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2336;
RG US DOE Joint Genome Institute;
RA Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA Dyer D.W., Inzana T.J.;
RT "Complete sequence of Haemophilus somnus 2336.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000947; ACA31021.1; -; Genomic_DNA.
DR RefSeq; WP_012340449.1; NC_010519.1.
DR AlphaFoldDB; B0UU13; -.
DR SMR; B0UU13; -.
DR STRING; 228400.HSM_1290; -.
DR EnsemblBacteria; ACA31021; ACA31021; HSM_1290.
DR GeneID; 56964945; -.
DR KEGG; hsm:HSM_1290; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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..831
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335477"
FT DOMAIN 330..500
FT /note="tr-type G"
FT REGION 1..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..346
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 364..368
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 386..389
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 440..443
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 476..478
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 339..346
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 386..390
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 440..443
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 831 AA; 91334 MW; 1DCA9F7B613E7B1F CRC64;
MADEIKKENA PKKLSIQRRT KTTVSGTSTT GKSKEVQVEV RKKRTVTTDL ERKAQEQAKL
KAKEEAEKRA AEEKLAEKAK REAEKAKAEQ IKIEKAKAEQ AKASKKNVDV EKEKRRAEEA
ELRRKADELA RQKAEEKAQK AAEEAKRYAD FDDSDNDNGK LDDYSDYHLT SSYALEAENE
EERRNENRGR SKNKVVKAKK GGRDDENGNK NERQSDRRNQ KDVKGKGKHA KKASALQQAF
TKPAQVAKAD VVIGETITVA ELAAKMAVKA TEIIKTMMKM GEMVTINQVI DQDTAQLVAE
EMGHKVILRK ENELEEMVME DRDVNAEKVH RAPVVTIMGH VDHGKTSLLD YIRKAKVAAG
EAGGITQHIG AYHVETNDGK MITFLDTPGH AAFTSMRARG AKATDIVVLV VAADDGVMPQ
TIEAIQHAKA ANAPLVVAVN KIDKPEANPD RVEQELLQHE VISEKFGGDV QFVPVSAKKG
LGIDDLLEAI LLQSEVLELT AVKDGMASGV VIESYLDKGR GPVATILVQS GTLNRGDIVL
CGFEYGRVRA MRDENGKDIQ SAGPSIPVEV LGLSGVPAAG DEATVVRDEK KAREVALYRQ
GKFREVKLAR QQKAKLENMF SNMAEGDVAE LNVIVKADVQ GSVEAIVQAL HELSTAEVKV
KVVGSGVGGI TETDATLAAA SNAIMVGFNV RADATARRVI ENENIDLRYY SIIYELLNEI
KAAMSGMLQP EFKQEIIGLA EVRDVFRHPK FGAIAGCMVT EGLVKRNNPI RVLRDNVVIF
EGELESLRRF KDDVSEVRSG MECGIGVKNY NDVKVGDQIE VFEVVEVKRA I
