IF2_RICCN
ID IF2_RICCN Reviewed; 831 AA.
AC Q92HF5;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RC0816;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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; AE006914; AAL03354.1; -; Genomic_DNA.
DR PIR; H97801; H97801.
DR RefSeq; WP_010977425.1; NC_003103.1.
DR AlphaFoldDB; Q92HF5; -.
DR SMR; Q92HF5; -.
DR EnsemblBacteria; AAL03354; AAL03354; RC0816.
DR KEGG; rco:RC0816; -.
DR PATRIC; fig|272944.4.peg.926; -.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000816; 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; 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..831
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137243"
FT DOMAIN 329..499
FT /note="tr-type G"
FT REGION 116..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 COMPBIAS 117..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 91072 MW; 031FAD99D9C6C8B4 CRC64;
MTDNQEIKPK KLTLGNSKLS LNKSFDSLTG AQSFVNAKSK TLVEVRKSST GSATTLSLNK
ERNSLDQTVI DANKEEFNRR LSILKKAAEQ SQLNDPLKIS TLSKLASINQ SANSKIEPLE
TDKEVEQKQQ NTEENKVEVS AKIVQDDEDI PSQIPKKKEE TFVKSPLVGK RTRYGIESEK
ELDKTAESKI IAPKIKLEEP KKFKKADLFN MLSDDESGSG RTRSLAAIKR AREKEKRKLV
SQAPEKVYRE VTIPEAIGVG DLANAMSERV ADVIKELMKL GILANASQTI DADTAELVAT
NLGHTVKRVQ ESDVENVLIS DDKVEDLRTR APVVTVMGHV DHGKTSLLDS LKSTDIAAGE
LGGITQHIGA YRVTLADGRA ITFIDTPGHE AFSEMRSRGA KVTDIVIIVV AADDGIKTQT
VEAINHAKAA GVPIIVAINK IDKPDIDIER VKNELYVHEI IGEEAGGDIM IIPISALKKI
NLDKLEEAIL LIAEMQDLKA NPFGSAAGVV IESKIEQGRG TLTTILVQRG TLRNSDIIIA
GTAYGKVKKM TNDKGLEIVE ATPSVPVEIQ GLNEVPFAGD KFNVVQNEKQ AKDIAEYRMR
LAKEKKISIA PRSSLEDLFL KASGNSKIKE LPLIIKGDVQ GSVEAISGSL LKLPSDEIKL
RILHSGVGPI TESDVSLAHA SSAIIVGFNV RAGANALTAA EKEKVDIRYY SIIYHLIDDI
KAIMSGMLDP IVREQYIGSA EMRQIFNITK VGKIAGSYVT KGIIKKGAGV RLLRDNVVIH
EGKLKTLKRF KDEVKEVREG YECGIAFENY QDIREGDTVE VFELIQEQRQ L
