IF2_FLAJ1
ID IF2_FLAJ1 Reviewed; 956 AA.
AC A5FJF9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Fjoh_1630;
OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=376686;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX PubMed=19717629; DOI=10.1128/aem.01495-09;
RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA Cheng Y.Q., Stein J.L.;
RT "Novel features of the polysaccharide-digesting gliding bacterium
RT Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL Appl. Environ. Microbiol. 75:6864-6875(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; CP000685; ABQ04662.1; -; Genomic_DNA.
DR RefSeq; WP_012023706.1; NZ_MUGZ01000017.1.
DR AlphaFoldDB; A5FJF9; -.
DR SMR; A5FJF9; -.
DR STRING; 376686.Fjoh_1630; -.
DR EnsemblBacteria; ABQ04662; ABQ04662; Fjoh_1630.
DR KEGG; fjo:Fjoh_1630; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_2_10; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000006694; 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; 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; 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.
FT CHAIN 1..956
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335468"
FT DOMAIN 454..622
FT /note="tr-type G"
FT REGION 53..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..470
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 488..492
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 510..513
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 564..567
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 600..602
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 59..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 463..470
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 510..514
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 564..567
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 956 AA; 104573 MW; F4260697EAFB1FE5 CRC64;
MSEERVIRIN KVLRELNISL ERAVDYLKDK GIAIDANPNA KISDSEFNIL QSQFAGDKGN
KEASKEVGEE KRKEKEALRV EREKEIEDKR RQEEERQKQQ EIIKARAVVS GPVQVGKIDL
NPKKPAAVSP EEPVKAEEPK TVTPTQTEKP VQKETVQSEP VAPVVSEEKK VEKPIITEKK
EVKAESSKTA QEPIISTDPT TAEETITTQY QKLSGTTLTG QTIDLSQFNK PKKKKEDPKI
TPNKPGTPGV GNNNNANKNK RKRIAPKPGT PGAPKPATGN APGTPNPNKI TPNSGGGFNA
NRNARPGFVK GNRPAIVAKV EPTEEEVKNQ IRETLEKLQG KGGKSKAAKY RRDKRETHRQ
KSDDEQRALD EGSKTIKVTE FVTVGEIAIM MDVPITKVIG TCMSLGIMVT MNQRLDAETL
TIVADEFGYD VEFITVDIEE AIEVVEDREE DLVTRAPIVT VMGHVDHGKT SLLDYIRKEN
VIAGESGGIT QHIGAYGVTL DNGQKIAFLD TPGHEAFTAM RARGAQVTDI AIIVIAADDD
IMPQTKEAIS HAQAAGVPII FAINKVDKPN ANPDKIKERL AGMNLLVEDW GGKIQSHDIS
AKTGLGVKEL LEKVLLEAEI LDLKSNPNKA AQGTVVEAYL DKGKGYVSTI LVQHGTLKIG
DYMLAGKHHG KVKAMHDERG HTVLTAGPST PVSVLGLDGA ATAGDKFNVF EDEKEAKQIA
SKRSQLMREQ SVRTQRHITL DEIGRRIALG QFKELNVILK GDVDGSVEAL SDSFSKLSTE
EVQINIIHKG VGAITETDVN LASASDAIII GFNVRPAGNA RQLADKEEID IRYYSIIYAA
IDDLKDAMEG MLAPEMKEEV LGTAEIREIF KISKVGSIAG CMVTDGKILR TSKIRVIRDG
VVVHTGELVA LKRFKDDVKE VTKGYDCGIQ IKGFNDIEIS DVIEAYHEVA IKKKLK
