IF2_TROWT
ID IF2_TROWT Reviewed; 803 AA.
AC Q83GT8;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=TWT_157;
OS Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX NCBI_TaxID=203267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Twist;
RX PubMed=12902375; DOI=10.1101/gr.1474603;
RA Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA Claverie J.-M.;
RT "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT reduced genome.";
RL Genome Res. 13:1800-1809(2003).
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; AE014184; AAO44254.1; -; Genomic_DNA.
DR AlphaFoldDB; Q83GT8; -.
DR SMR; Q83GT8; -.
DR STRING; 203267.TWT_157; -.
DR EnsemblBacteria; AAO44254; AAO44254; TWT_157.
DR KEGG; twh:TWT_157; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002200; 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..803
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137277"
FT DOMAIN 300..468
FT /note="tr-type G"
FT REGION 65..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..316
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 334..338
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 355..358
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 409..412
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 445..447
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 80..94
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 309..316
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 355..359
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 409..412
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 803 AA; 86480 MW; B04667EB105E0BFF CRC64;
MGVGLCGRGI VAKPRLYEVA SDLGTDSKTL MGILREMGEF VKSPSSALEP PVVRKLAKAF
AEKYPDKVEE KKEHTPPAPV VETPKAPPPL PRPIIRHAVR GVPSGAPRPG NNPYAPRQGM
GQLATPGPAT KRPVKFKAEG DKKPASTHRR VPAPLPQKRT PLRGRGAPGA FGRGNKPKSR
KSKTLKRQEF EMRDAPVIGG VTIPRGDGRV IRLMQGASVT DFAEKIDVLP ANLLSVLFHL
GEMATATESL DEATFEILAE EIGYKVQIVS PDDEDRALLE SFSVNLAAEH AEDSELDLAI
RPPVVTIMGH VDHGKTLLLD TIRNTNTLAE ESGGITQHIG AYQVSVGDRF VTFIDTPGHE
AFTAMRARGA KVTDIAVLVV AADDGIMPQT IEALDHARSA DVPIVVAVNK IDKEGANPAK
IRQQMTEFDV IPEEYGGDVM FIDISAKTGQ GVDALLEAIL LTADAALELR ANPDRTARGV
TIEAKLDAGR GAVATVLVQS GTLRVGDRVV TGCAYGRVRA MVDENGLPVE SAPPSRPVRV
QGLSSVPKAG DSFIVVAEDR QARQIAEKRE ANERNAQLAK SRKRVSLEDF TRAIQEGRVQ
SLNMIIKGDV SGAVEALEES LSKLDVGEEV SLRIIHRGVG AITESDVNLA TVDNAVVIGF
NVRPDRKARD RAAREGVDVR FYSVIYDAIE DIEKSLKGLL KPELEERKLG LAIVKEVFHS
SRVGTIAGCS VESGSITRNA KARLIRDGVV VVNDLTVTSL RRFKDDVTEV KSGFECGVGL
GSCDDIRIGD EIETIQIVEK PRA
