ID IF2_RUEST Reviewed; 835 AA.
AC Q1GCH2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=TM1040_2912;
OS Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=292414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM1040;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA Richardson P.;
RT "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL Submitted (MAY-2006) 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; CP000377; ABF65644.1; -; Genomic_DNA.
DR RefSeq; WP_011540225.1; NC_008044.1.
DR AlphaFoldDB; Q1GCH2; -.
DR SMR; Q1GCH2; -.
DR STRING; 292414.TM1040_2912; -.
DR KEGG; sit:TM1040_2912; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000000636; 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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 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; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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..835
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008339"
FT DOMAIN 332..500
FT /note="tr-type G"
FT REGION 1..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..348
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 366..370
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 388..391
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 442..445
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 478..480
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 341..348
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 388..392
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 442..445
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 835 AA; 89512 MW; 4BBADA009B0F4982 CRC64;
MSDSDGKKTL GLRGSGSRPG NVKQSFSHGR TKNVVVETKR KRVVVPKPGA GKGGAGGVAA
GDASRRPAGI SDAEMDRRLK ALQAAKAREA EEAAQREAEE KARAEERERR RAEQEAKERE
QREAEEKARQ KAEEEERKRQ EEAEAAKKRA AADKAAAAAP KSDAGVAPAR PAPGGAPKPA
AGPRKAERER EERGRGAKGR NDGGRRSGKL TLSQATGGEG GRQRSVASMK RKQERARQKA
MGQVEREKII RDVQLPEAIV VSELANRMAE RVADVVKALM NMGMMVTQNQ TIDADTAELI
IEEFGHNVVR VSDADVEDVI KEIEDKEEDL QPRPPVITIM GHVDHGKTSL LDAIRDAKVV
AGEAGGITQH IGAYQVTTDS GAVLSFLDTP GHAAFTSMRS RGAQVTDIVV LVVAADDSVM
PQTVEAINHA KAAGVPMIVA INKIDKPAAD PNKVRAELLQ HEVIVEAMSG EVQDVEVSAH
TGQGLDELLE AIALQAEILE LKANPNRAAQ GAVIEAQLDV GRGPVATVLV QTGTLRQGDI
FVVGEQYGKV RALINDKGER VKEAGPSVPV EVLGLNGTPE AGDVLNVTET EAQAREIAEY
REQAAKDKRA AAGAATTLEQ LMQKAKEDEN VSELPILVKA DVQGSAEAIV QAMEKIGNDE
VRVRVLHSGV GAITETDIGL AEASGAPVMG FNVRANASAR NTANQKGVEI RYYSVIYDLV
DDVKAAASGL LSAEIKENFI GYAEIKDVFK VSNVGKVAGC LVTEGVARRS AGVRLLRDNV
VIHEGTLKTL KRFKDEVAEV QSGQECGMAF ENYDDIRPKD VIEIFEREEV TRTLD
//
