IF2_RICTY
ID IF2_RICTY Reviewed; 831 AA.
AC Q68WI4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RT0539;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU04008.1; -; Genomic_DNA.
DR RefSeq; WP_011190989.1; NC_006142.1.
DR AlphaFoldDB; Q68WI4; -.
DR SMR; Q68WI4; -.
DR STRING; 257363.RT0539; -.
DR PRIDE; Q68WI4; -.
DR EnsemblBacteria; AAU04008; AAU04008; RT0539.
DR KEGG; rty:RT0539; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000604; 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_0000228238"
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; 91282 MW; A74438DBD1749897 CRC64;
MTDNQEIKPK KLTLGNSKLL LNKSFDSLTG VQSFVNAKSK TLVEVRKSSI GSTTTISLNK
ERNSLDQTVI DSNKEEFNRR LSILKKAAEQ SKLYDSAQIS TLSKLASINQ SVNSKNEQFT
TDKAVEQKQQ DIEDTKVEIG TKIVQDDEDI RSQIPNKKKE TFAKSLLVGM RTRYGIEAES
ALEKIGDNKV VVPKIKLEEP KKFKKADLFN MLSDDENGSG RTRSLASIKR AREKEKRKLV
SQIPEKVYRE VTIPEVIGVG DLANAMSERV ADVIKELMKL GILANASQTI DADTAELVAT
NLGHTVTRVQ ESDVENVLIN DDKVEDLRTR APVVTVMGHV DHGKTSLLDA LKSTDIAAGE
LGGITQHIGA YRVTLSDCKA ITFIDTPGHE AFSEMRSRGA KVTDIVIIVV AADDGIKTQT
VEAINHAKAA GVPIIVAINK IDKPDIDIER IKNELYVHEI IGEEAGGDVI FIPISALKKI
NLDKLEEAIL LISEMQDLKA SPFGLAAGVV IESKIEKGRG TLTTILVQRG TLRNGDIIIA
GTSYGKVKKM INDKGREILE ATPSVPVEIQ GLNEVPFAGD QFNVVQNEKQ AKDIAEYRIR
LAKEKKISVT SRSSLEELLL KASGNSKIKE LPLIIKCDVQ GSIEAIAGSL LKLPSDEIKL
RILHSGVGPI TESDVSLAHV SSAIVVGFNV RAGTNALTAA EKTKVDIRYY SIIYNLIDDV
KAIMSGMLDP IVREQYIGSV EIRQVFNITK IGKIAGSYVT KGIIKKGAGV RLLRDNVVIH
AGKLKTLKRF KDEVKEVREG YECGIAFENY EDIREGDTVE VFELVQEQRQ L
