IF2_ACIC5
ID IF2_ACIC5 Reviewed; 1061 AA.
AC C1F697;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=ACP_3327;
OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS 7670 / NBRC 15755 / NCIMB 13165 / 161).
OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC Acidobacterium.
OX NCBI_TaxID=240015;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 / NCIMB
RC 13165 / 161;
RX PubMed=19201974; DOI=10.1128/aem.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP001472; ACO31565.1; -; Genomic_DNA.
DR RefSeq; WP_015898360.1; NC_012483.1.
DR AlphaFoldDB; C1F697; -.
DR SMR; C1F697; -.
DR STRING; 240015.ACP_3327; -.
DR EnsemblBacteria; ACO31565; ACO31565; ACP_3327.
DR KEGG; aca:ACP_3327; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_0; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002207; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR PRINTS; PR00315; ELONGATNFCT.
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..1061
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202762"
FT DOMAIN 552..728
FT /note="tr-type G"
FT REGION 51..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..568
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 586..590
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 614..617
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 668..671
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 704..706
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 70..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..139
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..317
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 561..568
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 614..618
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 668..671
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1061 AA; 111261 MW; 4B29327B3E0DD481 CRC64;
MSKVRINDLA RELEVKSKAI LDALADCGVT EKKTHSSSLE ADEAVRVRAH FARGSRGAGQ
GGSRQQNEPK PKIDWSRVSK PGDVLKAIQE RNEQETVAAA RPAAVPVAPK APVSAPPAAR
PSAPRPAVTA APPPVAARPA GVQPGSQPAV SVQHGAEAQK PAPRRIVPQP RQPSAVVAPP
PAATPAIAAR PPAAPVAVKP PVTTAPIAQQ EKPAAPAAQE VKSALATGPS VPVAVSPSVV
VAAAPPPATA FQAPAAPAAP AASQSAPQEA KTPAAEAPPV APEKPAVPAP PQRRVIMPQT
GPRPVYTAPP PSASPVTPRP SGGGIQRGKP IFDRRPTGNS PGGPGGPGGG YGQRPSGPGG
RRPMHPTRNQ PGGGPPGGRP GFNNGPRPGF GQRPGGFGQR PGMGAPGLVP PPGDTPGRPQ
RPGAGQKRGG RSNQYPKSKE GPMKGFAPPS RFGGAQIPTE PLPITRTITV TEGISVKDLA
EKLGVRGKDL IATLLMRGVF VTVNQSLDGE LVKDVARQFG ADTTVISFED QMANEAFENL
LSQENPDELE LSRPPVVTVM GHVDHGKTSL LDAIRETDVA GGEAGGITQH IGAYKVRINK
EDSPAFGREI VFLDTPGHEA FTRMRARGAK VTDIVVIVVA ADDGVMPQTL EAVDHAKAAN
VPIIVAVNKI DKPEAQPDRV KKQLGDRGLV PEDWGGSTVF VDVSAKKRQN LDLLLEMICL
VADLGNLKAT PGRSAVGTVI EAKLDRGRGA VASVLVQNGT LRAQDSFIVG NTFGKIRAMF
DDRGRAIEEA GPSTPVEILG LENMPDAGDT FLVVADRDKA KGIAQYRQMK EREVQLAKSS
RVSLEGLAEQ IKQAGMKELP LILKGDVTGS VEVLADSLQK MSTEKVRIKV IHSGVGAITE
SDVLLASASN AIIIGFNVKP DRKSADLAEQ ENVEIRLHTI IYELQEEITK AMLGLLDPVF
KESYLGRAEV LNVFKIPKIG TIAGCRVLDG VLRRDSEIRL MRGGEQVFKG KLTSLKRFKD
DAKEVTNGME CGVGLNTSDI QVGDTVEAFT MERVAAELTA Q
