ID IF2_RICM5 Reviewed; 831 AA.
AC A8F223;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RMA_0853;
OS Rickettsia massiliae (strain Mtu5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=416276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mtu5;
RX PubMed=17916642; DOI=10.1101/gr.6742107;
RA Blanc G., Ogata H., Robert C., Audic S., Claverie J.-M., Raoult D.;
RT "Lateral gene transfer between obligate intracellular bacteria: evidence
RT from the Rickettsia massiliae genome.";
RL Genome Res. 17:1657-1664(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000683; ABV84959.1; -; Genomic_DNA.
DR RefSeq; WP_012152932.1; NC_009900.1.
DR AlphaFoldDB; A8F223; -.
DR SMR; A8F223; -.
DR KEGG; rms:RMA_0853; -.
DR HOGENOM; CLU_006301_10_2_5; -.
DR Proteomes; UP000001311; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 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.
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_1000057661"
FT DOMAIN 329..499
FT /note="tr-type G"
FT REGION 338..345
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 363..367
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 385..388
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 439..442
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 475..477
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 338..345
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 385..389
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 439..442
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 831 AA; 91240 MW; 17745C0A529B77AD CRC64;
MTDNQEIKPK KLTLGNSKLS LNKSFDSLTG AQSFVNANSK TLVEVRKSST GSATTLSLNK
ERNSLDQTVI DANKEEFNRR LSILKKAAEQ SKLNDPSKIS TLSKLASINQ SANSRIEPLE
TDKEVEPKQQ NTEENKVEVS AKIVQDDEDI PSQIPKKKED IFVKSPLVGM RTRYGIESEK
ELDKTADRKI VAPKIKLEEP KKFKKADLFN MLSDDESGSG RTRSLASIKR AREKEKRKLV
SQAPEKVYRE VTIPEVIGVG DLANAMSERV ADVIKELMKL GILANASQTI DADTAELVAT
NLGHTVKRVQ ESDVENVLIS DDKVEDLRTR APVVTVMGHV DHGKTSLLDA LKSTDIAAGE
LGGITQHIGA YRVTLADGRA ITFIDTPGHE AFSEMRSRGA KVTDIVIIVV AADDGIKTQT
VEAINHAKAA GVPIIVAINK IDKPDIDIER VKNELYVHEI IGEEAGGDVM VIPISALKKI
NLDKLEEAIL LIAEMQDLKA NPFGAAAGVV IESKIEQGRG TLTTILVQRG TLRNSDIIIA
GTSYGKVKKM INDKGLEILE ATPSVPVEIQ GLNEVPFAGD KFNVVQNEKQ AKDIAEYRMR
LAKEKKISIA PRSSLEDLFL KASGNSKIKE LPLIIKGDVQ GSVEAISGSL LKLPSDEIKL
RILHSGVGPI TESDLSLAHA SSAIIVGFNV RAGANALTAA EKEKVDIRYY SIIYHLIDDI
KAIMSGMLDP IVREQYIGSA EIRQIFNIIK VGKIAGSYVT KGIIKKRAGV RLLRDNVVIH
EGKFKTLKRF KDEVKEVREG YECGIAFENY EDIREGDTVE VFELIQEQRQ L
//
