IF2_SYNFM
ID IF2_SYNFM Reviewed; 962 AA.
AC A0LHL8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Sfum_1228;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
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., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-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; CP000478; ABK16920.1; -; Genomic_DNA.
DR RefSeq; WP_011698091.1; NC_008554.1.
DR AlphaFoldDB; A0LHL8; -.
DR SMR; A0LHL8; -.
DR STRING; 335543.Sfum_1228; -.
DR EnsemblBacteria; ABK16920; ABK16920; Sfum_1228.
DR KEGG; sfu:Sfum_1228; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR OMA; VAMSKID; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001784; 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; 2.
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..962
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008359"
FT DOMAIN 455..624
FT /note="tr-type G"
FT REGION 122..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..471
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 489..493
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 510..513
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 564..567
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 600..602
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 186..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 464..471
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 510..514
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 564..567
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 962 AA; 106191 MW; 48FAF7018CD55F73 CRC64;
MTRMRVHELA KELNMDNKDL IDRILKLGIQ VKNHMSTLTD SAVLKIRQQF SEAKTETVEE
KRIGRAVIRR RKKLTEGESA AAPAEGEERV ASEALPVEAE MPAQPVEAPE LIAEPISKLP
PEVGVAQPQL PEEPEPAPEP LIPAVKPEEA AASELAVEPQ TVVPPVAAPA AEVKPARPPM
EAPAPARKPP EEKETKVKHA EPESLAEPLP SPAPVELTLV PAESAAGQVA ERTDEEEEED
DKARPKKAKK RRRKKVRKDE PARIIKLPEI IPEEPEEEAV LPAHLATRIQ VKTEEVEVKE
APRKKRPRPE EFEKEAAERK AKGTRRKEVF EREDLYSKQE IAAQDDRGRL KGDKRRPFAK
EPARPEIAVV KPGKRKIRVD EAITVANLAK QMGIKATELI KKLLLLGLPA NINQAVDFDT
AALLASEFEF EVEKTGFEEE ELLQVREDRV EDLIRRPPVI TVMGHVDHGK TSLLDAIRDT
NVIGGEAGGI TQHIGAYYVM LPNGNVVFLD TPGHEAFTSM RARGAKVTDI VILVVAADDG
VMQQTIEAIN HAKAAEVPII VAINKVDKPN ANIDRVKREL AEHGLIPEEW GGNVTMVGIS
AKKRTGIEEL LEMVLLQAEL LELKANPAKP ARGRVIEAKL DKGRGPVATI LIQEGTLRTG
DVYLCGVNSG RVRNMFSDRG QRLDEAGPSM PVEVLGLSGV PNAGDDFITL PDERQAKMIA
EHRLVKLREK ELSRTSKVTL ESLFEQIQEG EIKELNLILK ADVHGSLEAI TDSLLKLSTP
EVKVSLIHFG TGAVIETDVM LASASNAIVI GFNVRSETKV QELADQENVD VRYYDVIYQL
LSDVKDAMVG MLEPVFKENV IGRAEVRQTF QVPKIGMIAG SFVLEGRVER NAKCRVLRDH
VVTYDGKISS LRRFKDDAKE VKAGFECGIG VENFNDIKVG DILEVYELQE MKPVLESPPG
DK
