IF2_POLSJ
ID IF2_POLSJ Reviewed; 968 AA.
AC Q12AU7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Bpro_2426;
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX NCBI_TaxID=296591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500;
RX PubMed=18723656; DOI=10.1128/aem.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE44345.1; -; Genomic_DNA.
DR RefSeq; WP_011483343.1; NC_007948.1.
DR AlphaFoldDB; Q12AU7; -.
DR SMR; Q12AU7; -.
DR STRING; 296591.Bpro_2426; -.
DR PRIDE; Q12AU7; -.
DR EnsemblBacteria; ABE44345; ABE44345; Bpro_2426.
DR KEGG; pol:Bpro_2426; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; RDVMMAG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001983; 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..968
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335498"
FT DOMAIN 468..635
FT /note="tr-type G"
FT REGION 305..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..484
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 502..506
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 523..526
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 577..580
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 613..615
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 327..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 477..484
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 523..527
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 577..580
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 968 AA; 103487 MW; C21A6D6B4C8E6460 CRC64;
MSSTTTVAEF AAELNKPTAT LIEQLTSAGV AKVQASDHLS EVDKQKLLGY LQASHGTVTA
ERKKITLVKK STTEIKQADA TGKARTIQVE VRKKRTFVKR EDGSDLPAEE VQPEVVAAPQ
VPVIDDAELI RREEEASRHA ELLRRQEAEL AEKRRLREEL DAKEAARELE RQAAAESAKA
AAEAAEAAKK AKPVTGKAKE VAQPAGAEAS RAAAETAVAE EAAATKAADA AVVQAAAKAK
ATAEFQADAA KAQDLQERRR KAEAEAAGIR AMMSAPKRVL VPHVDPKAAI KGTLHKPAVA
PGAAKPAAAA GAPGAPGAAG KKEVKSENLS STWKDDAAKK KGIPSRGATA VPGRGNFRSG
PRGRRSNDRD ARPESTFVAP TEFKVIEVHV PETITVAELA HKMSVKSSEV IKHLMKLGQM
VTINQPLDQD TAMIVVEEMG HKAITAALDD PEAFTDDDVQ GQQAEALPRA PVVTVMGHVD
HGKTSLLDYI RRAKVAAGEA GGITQHIGAY HVETPRGMIS FLDTPGHEAF TAMRARGAQA
TDIVILVVAA DDGVMPQTKE AIKHAKAAGV PIVVAINKID KADANMDRVK GELVTEEVIP
EEFGGESPFV GVSARTGEGV DTLLEQVLLQ AEVLELRAPV EALAKGLVIE AQLDKGRGPV
ATVLIQSGTL KTGDVVLAGS TYGRVRAMLD ENGKPIKTAG PSIPVEIQGL TEVPQAGDEF
MVMTDERRAR EIATYRAGKF RNTKLAKQQA SKLENMFSDI SAGEVKMLPI IIKADVQGSQ
EALAQSLLKL STDEVKVQLV YSGVGGISES DVNLAIASKA VLIGFNTRAD AQARKQAENN
GIDIRYYNII YDAVDELKAA MSGMLTPDKK EEVIGTAEIR QVFKVSKIGS IAGCMVTAGI
VRRTARLRLL RDNVVIFTGE LDSLKRFKDD VKEVKESFEC GLNIKNYNDI QEGDILEFFE
IKEVARTL
