IF2_MAGSA
ID IF2_MAGSA Reviewed; 872 AA.
AC Q2VZV0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=amb4071;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP007255; BAE52875.1; -; Genomic_DNA.
DR RefSeq; WP_011386422.1; NC_007626.1.
DR AlphaFoldDB; Q2VZV0; -.
DR SMR; Q2VZV0; -.
DR STRING; 342108.amb4071; -.
DR EnsemblBacteria; BAE52875; BAE52875; amb4071.
DR KEGG; mag:amb4071; -.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000007058; 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; 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; PF03144; GTP_EFTU_D2; 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.
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..872
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008266"
FT DOMAIN 371..539
FT /note="tr-type G"
FT REGION 130..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..387
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 405..409
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 427..430
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 481..484
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 517..519
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 130..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..192
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 380..387
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 427..431
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 481..484
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 872 AA; 93830 MW; F9FE70A3DEDBC583 CRC64;
MSDSQDQDRK APLKLTQPGK LELKKTVETG QVRQSFSHGR SKVVTVEVRK KRTFTSAGGA
MHEIKDGVHS VAEADLAAAV AKVEAASRAA SAHDLTTGEK AARAKALQDA LRHEEEVRAR
AEEEAIRHAA EEEAARAAEE EAARLAEEEA ARRAAEPQSE PEAAAPAAEP VAPTAPVAAA
PAPAPATPVA PAQPKPVAAA APAGDATAVP RARTEEEEEE EERAKKRAAA HKPAPVKRTE
PRRRTGKLTI TDALTDDDRS ERGRSLAAVK RARERERLKH MQKGSEKVIR EVIVPESITV
QELANRMAVR GADVIKCLMR LGVMATINQN IDADTAELVV TEFGHNMKRV SEADVLVGLE
GEADTDEVLF TRPPVVTVMG HVDHGKTSLL DALRATDVVS GEAGGITQHI GAYQVTMSSG
DKITFIDTPG HEAFTAMRAR GAKVTDIVVL VVAADDGIMP QTVEAIRHAK AAGVPIIVAI
NKIDKPGATP EKVRQELLQH ELVTEELGGD VLAIEVSAKK RLNLEKLEEA ILLQAEILDL
KANPTRAAQG VVVEAKMEKG RGSVATVLVQ KGTLKVGEVF VAGAEWGRVR ALVDDHGNSI
KEAGPSTPVE VLGLQGTPAA GDDFVTVEDE ARAREIAGYR SRMDREAKAK LAQRGTLEQM
FSAIKSGEAQ ELPVVIKGDV QGSIEAISST LEKMGNENVK VRILHAAVGA INESDITLAK
ASNGLLIGFN VRANPQARDM ARRDGVDIRY YSIIYDVTDD LKKMLSGMLA PELREKFLGY
ASIREVFNIT KVGKVAGCMI TEGTVKRGAK VRLLRDNVVI HTGDLGQLKR FKDDVKDVRE
GYECGMSFTN YEDIRVGDVI ECFEIEEIAV TL
