IF2_POLAQ
ID IF2_POLAQ Reviewed; 920 AA.
AC A4SY78;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Pnuc_1227;
OS Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=312153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1;
RX PubMed=22675600; DOI=10.4056/sigs.2395367;
RA Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT "Complete genome sequence of Polynucleobacter necessarius subsp.
RT asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP34442.1; -; Genomic_DNA.
DR RefSeq; WP_011903067.1; NC_009379.1.
DR AlphaFoldDB; A4SY78; -.
DR SMR; A4SY78; -.
DR STRING; 312153.Pnuc_1227; -.
DR EnsemblBacteria; ABP34442; ABP34442; Pnuc_1227.
DR GeneID; 31481614; -.
DR KEGG; pnu:Pnuc_1227; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000231; 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.
FT CHAIN 1..920
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335499"
FT DOMAIN 418..585
FT /note="tr-type G"
FT REGION 149..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..434
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 452..456
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 473..476
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 527..530
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 563..565
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 149..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 427..434
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 473..477
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 527..530
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 920 AA; 98348 MW; AF512CF9A460DCC7 CRC64;
MATTVKVLAK ELKRTAPDLL EQLKAAGIEK GSEDDSITEK DKTVLLEHLQ KEHGSAETGA
RKKITLIKRE NSEIRQADSA GRTRTVQVEV RKKRVLVKRS DEAAALEVEE APAKVIAPTE
PVKSILSAEE LEKRAAEATR QAELLARQEA EMKAAEEARQ KEVAAPVVEK EEKPVDNAPD
AAATAAEKKA TADKAAKDLA ATKEKELADI RVRRAAAEAE ALAIRDMMSA PARVLKAPSE
IAAEEAKKGT LHKPAKPEGA DDKKKAVAKV GGKTIKSAET SSTWQEEGAK KPGGLKTRGD
SSGGVGGWRS GGGRKKQRQI AEANVDTNFQ VPTEPVVRDV HVPETITVAE LAHAMAVKSA
EVIKLLMGMG QMVTINQVLD QDTAMIIVEE MGHTAHAAKL DDPDLDLGTD GHDAELLPRP
PVVTVMGHVD HGKTSLLDKI RAAKVATGEA GGITQHIGAY HVETPRGMIT FLDTPGHEAF
TAMRARGAKA TDIVILVVAA DDGVMPQTKE AIHHALAGGV PIVVAINKID KPEANSERVK
TELVAEQVVP EEYGGDVPFI PVSAKTGEGI DALLENVLLQ AEILELKAAK DAPAQGLVIE
ARLDKGKGPV ATILVQSGTL KRGDMLLAGS TYGRVRAMLD ENGKPCNEAG PSIPVEIQGL
GDVPAAGESV QVVPDERKAR EIALFRQGKF RDVKLAKQQA FKLETMMENM EEGAVEAKLL
PVIIKADVQG SQEALAQSLM KLSTPEVKVQ IVHAGVGGIT ETDVNLAVAS KAVIFGFNSR
ADAAARKLAE NNGVDIRYHN IIYDAVDEVK LALSGMLTPD KKEEITGLVE IRQVFLVSKV
GAIAGCLVVD GIVKRTSSVR LLRDNVVIWT GELDSLKRFK DDAKEVRAGV ECGLSLKGYN
DIKEGDQLEV FEVTEVARSL
