IF2_SINMW
ID IF2_SINMW Reviewed; 885 AA.
AC A6UF29;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Smed_3441;
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL Submitted (JUN-2007) 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; CP000738; ABR62259.1; -; Genomic_DNA.
DR RefSeq; WP_012067639.1; NC_009636.1.
DR RefSeq; YP_001329094.1; NC_009636.1.
DR AlphaFoldDB; A6UF29; -.
DR SMR; A6UF29; -.
DR STRING; 366394.Smed_3441; -.
DR EnsemblBacteria; ABR62259; ABR62259; Smed_3441.
DR GeneID; 61610992; -.
DR KEGG; smd:Smed_3441; -.
DR PATRIC; fig|366394.8.peg.6691; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001108; 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; 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..885
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008340"
FT DOMAIN 383..550
FT /note="tr-type G"
FT REGION 1..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..399
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 417..421
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 438..441
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 492..495
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 528..530
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 38..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..96
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 392..399
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 438..442
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 492..495
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 885 AA; 96136 MW; FF65B24A0C778CE9 CRC64;
MTDNKDDKTI SVAGKKTLTL KPSGVTQGTV RQDMGRGRTK AVVVETKRTR SPLKHKDERP
ITPVAAAPAA ARPAEQRPMP PQPSGRPAPQ PQPHQPRQEQ NRPRGGVVLN DLSASEMEAR
RHALAAAQIR DAEEAKRRAE EEVRRRREEE ERIAREKEEA ARRAAEEAAR PAVEAEKVEE
KVEAATPAVA ETRPLSERPA PAATPPAPAG VAPRGRRAGE DEEGERRHSS AGAPRGKVVR
PEPAKPAPRA KGDEGRRQGK LTLTAAVDED GSQRGRSLSA MRRRQEKFKR SQMQETREKI
SREVILPETI TIQELSQRMS ERAVDVIKFL MKEGQMMKPG DLIDADLAEL IAGEFGHTVK
RVSESDVEEG IFNISDADDE MHARPPIVTI MGHVDHGKTS LLDAIRHANV VAGEAGGITQ
HIGAYQVEQN GQKITFIDTP GHAAFTAMRA RGAQATDIAI LVVAADDSVM PQTIESINHA
KAAGVPIIVA INKIDKPSAD PQKVRTELLQ HEVFVESMGG EVLDVEVSAK NQTNLDKLLE
AILLQSEILD LKANPNRTAE GTVVEAELDR GRGAVATVLV QKGTLTPGQI IVAGDQWGRV
RALVNDKGEH VKSAGPSTPV EVLGLSGTPA AGDRFAVVES ESRAREISEY RQRLAREKAV
ARQSGSRGSL EQMMTQLQTS GVKEFPLVIK GDVQGSIEAI SGALEKLGTD EVRARIVHSG
AGGITESDVS LAEASNAAII GFNVRANKQA RDASERAGIE IRYYNIIYDL VDDVKAAMSG
LLSPERRETF LGNAEILEVF NITKVGKVAG CRVTEGKVER GVGVRLVRDN VVIHEGKLKT
LKRFKDEVSE VQSGQECGMA FENYEDIRAG DTIECFRVEH VTRTL
