IF2_TREDE
ID IF2_TREDE Reviewed; 896 AA.
AC Q73NP6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=TDE_1106;
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(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; AE017226; AAS11595.1; -; Genomic_DNA.
DR RefSeq; NP_971714.1; NC_002967.9.
DR RefSeq; WP_002682412.1; NC_002967.9.
DR AlphaFoldDB; Q73NP6; -.
DR SMR; Q73NP6; -.
DR STRING; 243275.TDE_1106; -.
DR PRIDE; Q73NP6; -.
DR EnsemblBacteria; AAS11595; AAS11595; TDE_1106.
DR GeneID; 2740236; -.
DR KEGG; tde:TDE_1106; -.
DR PATRIC; fig|243275.7.peg.1065; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_12; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 115308at2; -.
DR Proteomes; UP000008212; 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..896
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228257"
FT DOMAIN 375..544
FT /note="tr-type G"
FT REGION 1..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..391
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 409..413
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 430..433
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 484..487
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 520..522
FT /note="G5"
FT /evidence="ECO:0000250"
FT REGION 877..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 384..391
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 430..434
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 484..487
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 896 AA; 98141 MW; 1A6C6B19A82A6283 CRC64;
MDIENTNKPD VILNKKSSKA ADSKPESGKT DSKRKVVVKV SKTSAGKSKK PESSSEESSG
GKASGKQVIS VKKASSQSSK PAEASVKEKK PDERLEETKK TAPRFEDKKS DAPSAQNEKR
SFDSAKKEEK QTERKKPTPS SIDSIDFASK RPNVKAGNLA DSGRRNNRGQ GNRPQRPGGQ
GQGQPGQGRR RESNFSGAQA RAYSDGKKQG FRTGQGGQQG RPGDRPQNRP GFGGPRPGAA
PAPIPVEKNK AQTNKKAHKA KKEIYNKKNK EEEFFEERLL NQKKKQKEKI HNIPKQIEIM
ESISVSELAK KMNLKASELI GKLMGMGMMV TMNQSIDADT ATILASEYDC DVKIVSLYDE
TVIESKEDDL SELQPRPPVV TIMGHVDHGK TKTLDAIRSS NVIAGEFGGI TQHIGAYTVN
THGGKITFLD TPGHEAFTMM RARGAEITDI VVLVVAADDG VMPQTIEAIN HARDAKVPII
VAVNKVDKPE ANVDKVKTRL SELGLMPEEW GGDTMFVEIS ALKKLGLDNL LDTILLQAEV
LELKANYTCN AEGKVIESRI DHGRGVVATI IVQRGTLRTG DPYVAGIYSG RVRAIFNDRG
EKIDEATPSM PVEILGLEGM PNAGDPFQVT DSERIARQIS DKRQELKRFE DSRNVKKVTL
DNLYETIHDG EILELKVIIK GDVQGSVEAL KQSLEKLSTP EIRLNVIHAS AGAINDSDVM
LAAADSNALI IGFNVRPTPQ AKLLADQEKV DIRKYTVIYK AVEEIQLAME GMLSPDIKEQ
VIGMVEVRNT FKVPKIGKIA GCYVLEGVVK RNCAVHVIRD GIVVHSGKLS SLKRFKDDAK
EVAAGFECGI GIEDFNDIQV DDQLEIIEMI QVARKLSDSE KYKAPEIKEE GTETDE
