IF2_AMOA5
ID IF2_AMOA5 Reviewed; 908 AA.
AC B3EUG6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Aasi_0139;
OS Amoebophilus asiaticus (strain 5a2).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Amoebophilaceae;
OC Candidatus Amoebophilus.
OX NCBI_TaxID=452471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5a2;
RX PubMed=20023027; DOI=10.1128/jb.01379-09;
RA Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA Rattei T., Horn M.;
RT "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT reveals common mechanisms for host cell interaction among amoeba-associated
RT bacteria.";
RL J. Bacteriol. 192:1045-1057(2010).
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; CP001102; ACE05585.1; -; Genomic_DNA.
DR RefSeq; WP_012472355.1; NC_010830.1.
DR AlphaFoldDB; B3EUG6; -.
DR SMR; B3EUG6; -.
DR STRING; 452471.Aasi_0139; -.
DR EnsemblBacteria; ACE05585; ACE05585; Aasi_0139.
DR KEGG; aas:Aasi_0139; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_2_10; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001227; 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..908
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093756"
FT DOMAIN 407..577
FT /note="tr-type G"
FT REGION 123..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..423
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 441..445
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 463..466
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 517..520
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 553..555
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 123..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 416..423
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 463..467
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 517..520
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 908 AA; 100503 MW; C99732778CCBE9CD CRC64;
MVEEKTIRLS QVARKLNVAT TTIAAYLLEK GFRVENKPNT KITLEQYKIL AEEFADSAMD
KEEAAELVIG QSYEKEPKVI AKQQEPIKHV HPKEKQVEIE KISLPVIDAP TIIEHKIIEH
KTEEPPILQP ELPTEEKEEL EVIESPQAPQ EELKPELETE VQEQDKEIQQ ELDDTAKVEQ
APITKGPEKI DFSKQGEFKG VTVLGKIELA EKKEPKKFQQ VASSDIDKKN KKRPRKRVAS
ETGLPSSGKR EEEANRYKPK GKVTNKTPEA PKTAVSEKQI QDQIKSTLAK LGGGKNVASR
AKYRREKRSL LAEEQAEERL QAAKDAKKLQ VTEFIAASDL ASLMGVSINQ LLSTCMNLGM
LVSINQRLDA EAITIIADEF GYQVAFTDVK TQELEEEEEA NPEDLVERAP IVTIMGHVDH
GKTSLLDYIR NTQITKTEAG GITQHIGAYE VVTESGKHIA FLDTPGHEAF TAMRARGAKL
TDIAIIVIAA DDGVRPQTKE AINHAKLAGV PIIIAINKMD KPQANPERVK EELAHLNILV
EDWGGKYQSQ GVSAISGEGV KELLEKILFE AELLELKANS HKKARGTVIE ASLDQGRGYL
ATIMVQDGNL RIGDVVLAGA YYGKIKAMFD YQGKPVKQAG PSTPMQILGL NGAPQAGDLF
RAMNTEKEAR DIATQRQQIL REQGFRTKTH ITLDEIGRRL AIGNFKELNI ILKGDVDGSV
EALSDSLLKL STEEIKVTIL HKGVGAIVES DILLAAASDA IIIGFQVRPT PPVRKLAEKE
GIEIRLYSII YDAINDIKDA MEGMLAPTIE EIITGSASVR EIFKITGTGT VAGCYVTEGY
IKKNNSIRVI RDGIVIYTGS IKHLKHFKEE MQQVKTGFEC GISITNFNDL KVNDVIEGFE
QKEVERKL
