IF2_POLNA
ID IF2_POLNA Reviewed; 992 AA.
AC A1VNU2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Pnap_2011;
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2;
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT tar-contaminated sediment, reveals physiological and metabolic versatility
RT and evolution through extensive horizontal gene transfer.";
RL Environ. Microbiol. 11:2253-2270(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; CP000529; ABM37320.1; -; Genomic_DNA.
DR RefSeq; WP_011801400.1; NC_008781.1.
DR AlphaFoldDB; A1VNU2; -.
DR SMR; A1VNU2; -.
DR STRING; 365044.Pnap_2011; -.
DR EnsemblBacteria; ABM37320; ABM37320; Pnap_2011.
DR KEGG; pna:Pnap_2011; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; RDVMMAG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000644; 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..992
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335497"
FT DOMAIN 492..661
FT /note="tr-type G"
FT REGION 154..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..508
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 526..530
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 547..550
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 601..604
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 637..639
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 351..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 501..508
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 547..551
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 601..604
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 992 AA; 105594 MW; 94A4EF6464EF9AE8 CRC64;
MSSTTTVAEF AAELNKSPAT LIEQLTSAGV AKVQASDPLS ESDKQKLLGY LHASHGTVAA
DRKKITLVKK STSEIKQADS TGRARIIPVQ TIKKRTFIKR DDGSDMPVEE AQPEVLVAPQ
VQAAADAELV RREDEANRHA ELLRRQEAEL TEKRRLRDEQ AAQEAARERE REAAAQKAQA
EAVAQAAAAA QAAALAAEAA KKVKPTIGKI FKPAPVAPTA PAITVEAQKV IDTAAAEKTS
KAAEAATAKA AETASLQAAA KAKATAEFQA DAAKAVDLQE RRRKAEAEAA GIRAMLSAPK
RVLVPHVDPK IAMKGTLHKP VVAPGAAKPA VPAAAAPAAP GAAGKKEVKS ENLSSTWKDD
AAKKKGIPSR GAPVVPGRGN FRAGPRGRRS SGRDVRPESN FVAPTEFKVL EVHVPETITV
SELAHKMSIK SSEVIKHLMK LGQMVTINQP LDQDTAMIVV EEMGHTALTA ALDDPEAFTA
DDVQGQQAEA LPRAPVVTVM GHVDHGKTSL LDYIRRAKVA SGEAGGITQH IGAYHVQTPR
GMVSFLDTPG HEAFTAMRAR GAQATDIVIL VVAADDGVMP QTKEAIKHAR AAGVPIVVAI
NKIDKPGINL ERVKGELVTE GVVPEEFGGD SPFVPVSAHT GAGIDDLLEQ VLLQAEVLEL
KASVDSLAKG LVIEARLDKG RGPVATVLVQ SGTLKAGDVV LAGSTYGRVR AMLDENGKPI
KTAGPSIPVE IQGLTEVPQA GDDFMVMTDE RRVREIATYR AGKFRNTKLA KQQASKLENM
FSDINAGEVK MLPIIIKADV QGSQEALAQS LLKLSTDEVK VQLVYSGVGG ISESDVNLAI
ASKAVLIGFN TRADAQARKQ AENNGIDIRY YNIIYDAVDE LKAAMSGMLT PDKKEEIIGN
AEIRNIFKVS KIGSIAGCMV TAGVVRRTAK VRLLRGNVVI FTGELDSLKR FKDDAKEVKE
GFECGLNLKN YNDIEVGDIL EFFEIKEVAR TL
