IF2_HYDCU
ID IF2_HYDCU Reviewed; 818 AA.
AC Q31GK5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Tcr_1123;
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA Tinkham L.E., Zeruth G.T.;
RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT XCL-2.";
RL PLoS Biol. 4:1-17(2006).
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; CP000109; ABB41718.1; -; Genomic_DNA.
DR RefSeq; WP_011370545.1; NC_007520.2.
DR AlphaFoldDB; Q31GK5; -.
DR SMR; Q31GK5; -.
DR STRING; 317025.Tcr_1123; -.
DR EnsemblBacteria; ABB41718; ABB41718; Tcr_1123.
DR KEGG; tcx:Tcr_1123; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF46955; SSF46955; 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..818
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008368"
FT DOMAIN 317..484
FT /note="tr-type G"
FT REGION 128..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..333
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 351..355
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 372..375
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 426..429
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 462..464
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 128..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 326..333
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 372..376
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 426..429
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 818 AA; 89603 MW; 6E4D333CF235261D CRC64;
MSQVSIKQFA ETLKLSVDKL LSQLEEAGVS GKKEADFLSD DEKMTLLNYL KGLHGEKVDA
PNKVTLKRKQ VQKLNLSSGA GKRTVNVEVR KKRTYVKKPE TVEEPVVEEP IVEEAVVDVP
EMDTAAETKA TKEAEAPKEK AAEAPVSPET ILDVVPEPVP VETDKKHKHD KKKQNKAPVK
EEPKHKGKPK PKEKQSKKTL AMSGDQSFGR RRHKGHKKSH NADNEHGFQK PVEKQVRDVP
LGETIKVSEL ADKMAVKATE VIKTMMGFGS MVTINQVLDQ ETAQLVVEEM GHKPVLVNEN
QIEDDVVNQD YNGETVQRSP VVTIMGHVDH GKTSLLDYIR KAKVAHGESG GITQHIGAYH
VETGHGGVTF IDTPGHEAFT AMRARGAKVT DVVVIVVAAD DGVMPQTKEA IQHAKAAKLG
MVIAINKMDK EGANPDRVMQ ELVSEEVVPE EWGGDTQFVR VSAKSGEGVD DLLDAILLQS
EILELEAPLE GPAKGVVVES RLDKGRGPVA TVLVQAGTLR KGDIALCGME YGRVRALVNE
TGEQVESAGP SIPVEVLGMS GVPVAGDDMI TVESERKARE VAMFRQSKHK EKKIARQQKS
KLDNMFNKME EGEIQNVNII LKADVQGSIE AIVDALVKLS NDEVKVSVVS SGVGGITETD
ANLALASDAL IFGFNVRADA KAKRLIDSEG IFLKYYSVIY EIIDEVKRAI EGKLAPDFKE
EIIGVADVRD VFKAPKIGLI AGCMVTEGMV KRNNPIRVLR DNIVIYQGAL ESLRRFKDDV
PEVRQGMECG IGVKDYNDVK VGDQIEVYER VEVKRTLD
