IF2_TOLAT
ID IF2_TOLAT Reviewed; 910 AA.
AC C4L8X4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Tola_2246;
OS Tolumonas auensis (strain DSM 9187 / TA4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Tolumonas.
OX NCBI_TaxID=595494;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA Beller H.;
RT "Complete sequence of Tolumonas auensis DSM 9187.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001616; ACQ93844.1; -; Genomic_DNA.
DR RefSeq; WP_015879312.1; NC_012691.1.
DR AlphaFoldDB; C4L8X4; -.
DR SMR; C4L8X4; -.
DR STRING; 595494.Tola_2246; -.
DR PRIDE; C4L8X4; -.
DR EnsemblBacteria; ACQ93844; ACQ93844; Tola_2246.
DR KEGG; tau:Tola_2246; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3064; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000009073; 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; 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; Reference proteome.
FT CHAIN 1..910
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202787"
FT DOMAIN 410..577
FT /note="tr-type G"
FT REGION 51..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..426
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 444..448
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 465..468
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 519..522
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 555..557
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 51..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 419..426
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 465..469
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 519..522
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 910 AA; 100014 MW; E65D97654CED1915 CRC64;
MADLSVKQLA IEVGTPVDRL VQQFKDAGLN KDADAMVTEH EKQALLEHLK KQHGADNAEP
KRMTLQRKTK GTLSVPGAGG KNKEVQIEVR KSKTYVHRSV IDEAQQQKEA EEKARQEAEK
TRQEELAKAE QARKDAEAKA RKEAEEKARK EAEARKQSTE AAADDAAKSP DEKARKVKAE
ADKRADENAK REAEALRKKQ EEEAQRKTEL EAQRKTELEA QRIAEEARRL AVENEGRWAA
EEEARRRAEL TDDVGEAASK FVKEAEAERE RQDESKGRRR TGVVKAKKSP HEEAREERNS
RARKGKRAKV HTPNSMQHGF QKPAQPVNRD IVVGETISVG ELAQKMAVKA VEVIKVMMKM
GAMATINQII DQETAQLVAE EMGHKVTLRR ENELEEAVLQ DRDSTATREG RAPVVTIMGH
VDHGKTSLLD YIRKAKVASG EAGGITQHIG AYHVDTENGS ITFLDTPGHA AFTAMRARGA
QATDIVVLVV AADDGVMPQT VEAIQHAKAA GVPIVVAVNK VDKPDADPDR VMNELTRYSV
IPEEWGGENQ FVKVSAKSGE GIDNLLNAIL LQSEVLELGA VRDAMASGVV IESRLDKGRG
PVATVLVQEG TLHQGDIVLC GFEYGRVRAM RDELGRSIDA AGPSIPVEIL GLSGVPSAGD
EATVVRDEKK AREVALYRQG KFRDVKLARQ QKAKLENMFA NMTEGEVSEL NVVLKADVQG
SVEAIADSLN KLSTDEVKVR IIGSGVGGIT ETDASLAAAS NAIVLGFNVR ADASARKIIE
SESIDLRYYS VIYDLIDEVR QAMSGMLAPE YKQQIIGLAE VRDVFRSPKF GAVAGCMVTE
GTVKRNSPIR VLRDNVVIYE GELESLRRFK DDVPEVKNGY ECGIAVKNYN DVRPGDQIEV
YETVEIQRTL
