IF2_ORITB
ID IF2_ORITB Reviewed; 848 AA.
AC A5CEN6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=OTBS_1568;
OS Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Orientia.
OX NCBI_TaxID=357244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boryong;
RX PubMed=17483455; DOI=10.1073/pnas.0611553104;
RA Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
RA Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J., Koh Y.-S.,
RA Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S., Kim I.-S.;
RT "The Orientia tsutsugamushi genome reveals massive proliferation of
RT conjugative type IV secretion system and host-cell interaction genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(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}.
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DR EMBL; AM494475; CAM80661.1; -; Genomic_DNA.
DR RefSeq; WP_011944946.1; NC_009488.1.
DR AlphaFoldDB; A5CEN6; -.
DR SMR; A5CEN6; -.
DR PRIDE; A5CEN6; -.
DR EnsemblBacteria; CAM80661; CAM80661; OTBS_1568.
DR KEGG; ots:OTBS_1568; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001565; 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; Reference proteome.
FT CHAIN 1..848
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335495"
FT DOMAIN 347..517
FT /note="tr-type G"
FT REGION 106..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..363
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 381..385
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 403..406
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 457..460
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 493..495
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 356..363
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 403..407
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 457..460
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 848 AA; 93393 MW; 1B51C6EF39BF71CB CRC64;
MTDKHNEEGK EKKLKLPSKM IIGKHVDSKK FKTSYFTSHN NSVTVEIKGG RKFSSSSSLP
HKINTQISTI DEFNEKISLL KKAASFAKSE EYRSNVTNFS STVEVTEQQT EAENSTNINL
SEQTIKNNSH QSSSNTIETT QEKKQNDDLS SNITPVEAIT QLEPNQKILQ NQQNSSSISL
NSIISKPQNK SSIENNVEFE TEATSTKSSA IWTKKNNSAK PKKSDIYQML DSDSKSKTRS
FAAIKRARDK EKRKLQNNAL TKKIYREVII PDTITVNELA LRMSEKLSDV MQALLKLGIK
ANINQSIDVD TAELIAISLG HSVKRTQDSD VENILHSDKD TQDSLLPRAP IITVMGHVDH
GKTCLLDALR STDVISTEAG GITQHIGAYK VNLPNNKSIT FIDTPGHEAF SEIRTRGAKV
TDIVVLVIAA NDGIKPQTIE AINHAKAAKV PILVAINKID APDANPDKVK NALLAHNIVP
EDLGGETLVV PISALKKINL DKLEEAILLL ADMLELKANP NALASGTVIE SQVDHKSGVI
ATILVQRGTL KIGDILIAGN GFGKVKRMIN DKNQQVNYAY PSDPVKILGL SQIPNAGDAV
AVVQNEKQAR SIVDYRIRKA KEEQDLKVHN ISLEELLKQA SANQFKELSL ILKTDVHGSL
EAIVASINKI VNDEVKIKIL HAAVGVINES DIILANASNA TILGFNVKID STASIKAERN
KTNIKYYSII YDLIDYVKSA VSGMLSPIIH EEYTGRAEVR AVFNITKVGK IAGCYVTKGY
IQRNSKVKLL RNNEVIFSGP LQTLKRFKEH TKEVKEGFEC GIELANYYDI NVGDIIEAFI
VTEEKAKL
