IF2_BACFN
ID IF2_BACFN Reviewed; 1015 AA.
AC Q5LIN1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BF0219;
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(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}.
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DR EMBL; CR626927; CAH05995.1; -; Genomic_DNA.
DR RefSeq; WP_005783920.1; NC_003228.3.
DR AlphaFoldDB; Q5LIN1; -.
DR SMR; Q5LIN1; -.
DR STRING; 272559.BF9343_0216; -.
DR PRIDE; Q5LIN1; -.
DR EnsemblBacteria; CAH05995; CAH05995; BF9343_0216.
DR KEGG; bfs:BF9343_0216; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_0_10; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000006731; 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; Reference proteome.
FT CHAIN 1..1015
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228169"
FT DOMAIN 514..684
FT /note="tr-type G"
FT REGION 124..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..530
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 548..552
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 570..573
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 624..627
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 660..662
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 260..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 523..530
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 570..574
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 624..627
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1015 AA; 112631 MW; 396DFD315CE1A40D CRC64;
MTIRLNKVTR DLNVGIATVV EFLQKKGYTV EANPNTKITE EQYAMLVKEF STDKNLRLES
ERFIQERQNK DRNKASVSID GYDKKEPEKT VADDVIKTVI PEDVRPKFKP VGKIDLDKLN
RKVEKEPVKE EPKPQPVAAE EKKVAEEVKP VVNEVKKEEV TVTPATSEPK PVKEEPKPVV
VEKPVETEKK VVEEVKKEEP KVVVSPEKTE KKEEKPVAEA PVTPVEKEEE GVFKIRPTEF
VSKINVIGQI DLAALNQSTR PKKKSKEEKR KEREEKEKLR QDQKKQMKEA IIKEIRKEDS
KQAKVVGKEN LDPNGKKKRN RINNNKEKVD VNNVASNFAH PTPNSERTNN NRGGNQQGGG
GQNRNRNNNN KDRFKKPVVK QEVSEEDVAK QVKETLARLT SKGKNKGAKY RKEKRDMASN
RMQELEDQEM AESKVLKLTE FVTANELASM MNVSVNQVIG TCMSIGMMVS INQRLDAETI
NLVAEEFGFK TEYVSAEVAQ AIVEEEDAPE DLEHRAPIVT VMGHVDHGKT SLLDYIRKAN
VIAGEAGGIT QHIGAYHVTL EDGRKITFLD TPGHEAFTAM RARGAKVTDI AIIIVAADDD
VMPQTKEAIN HAAAAGVPIV FAINKIDKPH ANPEKIKETL AQMNYLVEEW GGKYQSQDIS
AKKGLGVPEL MEKVLLEAEM LDLKANPNRN ATGSIIESTL DKGRGYVATV LVSNGTLKVG
DIVLAGTSYG RVKAMFNERN QRVAQAGPSE PVLILGLNGA PAAGDTFHVI ETDQEAREIA
NKREQLQREQ GLRTQKLLTL DEVGRRIALG NFQELNVIVK GDVDGSIEAL SDSLIKLSTE
QIQVNVIHKA VGQISESDVT LAAASDAIII GFQVRPSASA RKFAEQEGVD IRLYSVIYAA
IEEVKAAMEG MLAPEVKEVV TATIEVREVF HITKVGTVAG AVVKEGKVKR SDKARLIRDG
IVIFSGSINA LKRFKDDVKE VGTNFECGIS LVNYNDLKVG DMIETYEEVE VKQTL
