IF2_AZOC5
ID IF2_AZOC5 Reviewed; 1058 AA.
AC A8IG20;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-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=AZC_0020;
OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Azorhizobium.
OX NCBI_TaxID=438753;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC 13405 / ORS 571;
RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT caulinodans ORS571.";
RL Submitted (APR-2007) 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; AP009384; BAF86018.1; -; Genomic_DNA.
DR RefSeq; WP_012168551.1; NC_009937.1.
DR AlphaFoldDB; A8IG20; -.
DR SMR; A8IG20; -.
DR STRING; 438753.AZC_0020; -.
DR PRIDE; A8IG20; -.
DR EnsemblBacteria; BAF86018; BAF86018; AZC_0020.
DR KEGG; azc:AZC_0020; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000270; 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; 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; 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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..1058
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000071286"
FT DOMAIN 555..725
FT /note="tr-type G"
FT REGION 1..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..571
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 589..593
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 611..614
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 665..668
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 701..703
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..97
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 564..571
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 611..615
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 665..668
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1058 AA; 111350 MW; 2991D9BD2A1D8188 CRC64;
MNDTKTPGDK TLHPAPGKTL TLKRPVEQGT VRQSFSHGRS KSVVVEKVKR RVFAPGEAGA
PSGTPAAAPA ATPAPAAAAP RPATPAPAAP RPAAPATPAQ PAAEAKAPAP APTPAPAAPA
APVAEAPKVE APAPVAAKPE AAPAAPVAEA PKVEVPAPAP APAEPVAAQP AAPVAAAPAA
PARAPEAPRP AVSAPRPAAT TSSGSSSSSS RPAAGGAQRS GAAPQRPGTS GGPGRPGAPA
SGQRSGGPGS DRRGGPGGQN RPGQNRQGGS GVVLRTLTEE ERNARASALA DARVREVEER
RMAEERRIAE EEARRRAERE RAERAEREAA EARKREEESR RALEDESKRR AEQEARKRFG
EETGRSGGAS APSTSTARPL TPRPAGTTTT TGAPAAGEEE DRRPRRGGGV PPRPAAPVKL
PKSAGGEKHR GRLTVVTAQS GEEERQRSVA SFRRRTQRMT GHRGMQESKE KIVREVVLPE
TITIQELANR MSERAVDVIR MLMKQGQMVK ITDVIDADTA ELIAADLGHT VRRVSESDVE
EGLFDSADAP EDLLPRPPVV TIMGHVDHGK TSLLDSLRKA NVVSGEAGGI TQHIGAYQVT
SPLGGKITFI DTPGHAAFTA MRARGAKVTD IVVLVVAADD GVMPQTVEAI NHARAAKVPL
IVAINKIDKP DAKPERVRSE LLQYEVQVES MGGDTLEVEV SATKQINLDK LLEAISLQSE
VLDLKANPDR PAEGTVVEAK LDRGRGPVAT VLVQRGTLRV GDIVVAGAEF GRVRALITDT
GATTTEAGPS VPVEVLGFNG TPEAGDRLAV VESEARAREI TEYRQRQKRE KAAARSAVVR
GSLEQMMSQV RSTGRKEFPL IIKGDVSGSV EAIIGALEKL GNDEVQARII HSGAGGINES
DVTLAETSGA AIIGFNVRAN KEARDSAERA GIEIRYYNII YDLVDDVKKA MSGLLAPITR
ETMLGNALIL EIFNVSKVGK VAGCRVTDGT VERGQHVRLI RDNVVIHEGK LATLNRFKDA
VKEVLAGQEC GMSFENYQDM RAGDVIECYR VEVVQRSL
