IF2_PHOV8
ID IF2_PHOV8 Reviewed; 1003 AA.
AC A6L030;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BVU_1355;
OS Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Phocaeicola.
OX NCBI_TaxID=435590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC 11154;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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; CP000139; ABR39044.1; -; Genomic_DNA.
DR RefSeq; WP_011965153.1; NC_009614.1.
DR AlphaFoldDB; A6L030; -.
DR SMR; A6L030; -.
DR STRING; 435590.BVU_1355; -.
DR PRIDE; A6L030; -.
DR EnsemblBacteria; ABR39044; ABR39044; BVU_1355.
DR KEGG; bvu:BVU_1355; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; BVUL435590:G1G59-1413-MON; -.
DR Proteomes; UP000002861; 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..1003
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008200"
FT DOMAIN 502..672
FT /note="tr-type G"
FT REGION 61..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..518
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 536..540
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 558..561
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 612..615
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 648..650
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 139..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 511..518
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 558..562
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 612..615
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1003 AA; 111109 MW; E4468573F2A85003 CRC64;
MTIRLNKVTR DLNVGITTVV EFLQKKGYTI EASPNAKITE EQYAVLVKEF STDKNLKIES
EKFSQERQNK DRNKASISIE GFESKKEKEE VVKTVIPEEA RPKLKQVGKI DLDNLNKKTA
PKVVEPAAKV IEQTPKAEPV VEKVVERKET PQPEKETPKP VVVEEKKPEP APQPAPAPVL
EEKKEPKIEK TEEKTPQVKE MEKETPEAAP VQEKEEDDVF KIRPTEFKSK INVVGQIDLA
ALNQSTRPKK KSKEEKRKER EEKDKQRQEQ RKLMKDAIIK EIRKGDDKIS KNSVNDDAAK
KKKRNRINKE RVDINAAGTT NAGGASNNNQ RNDNANRPNR NNNSKPNGNN NQGGGKFNKD
RFKKPVVKAE VSDEDVAKQV KETLARLTNK TKNKAAKYRK EKRENVQNRL MEQEEMEQED
SKILKLTEFV TANELASMMD IPVTQVIATC MSIGIMVSIN QRLDAETINL VAEEFGYKTE
YVSAEVAQAI TEEEDNEEDL QPRAPIVTVM GHVDHGKTSL LDYIRKANVI AGEAGGITQH
IGAYNVKLED GRHITFLDTP GHEAFTAMRA RGAKVTDIAI IIVAADDNVM PQTKEAINHA
MAAGVPIVFA INKVDKPHAN PDKIKEELAA MNFLVEEWGG KYQSQDISAK KGTGVHDLLE
KVLLEAEMLD LKANPDRKAT GSIIESSLDK GRGYVATMLV ANGTLKMGDI VLAGTSYGKV
KAMFNERNQR IKEAGPSEPV LILGLNGAPA AGDTFHVIDT EQEARDIANK REQLQREQGL
RTQKLLTLDE VGRRLALGDF HELNVIVKGD VDGSVEALSD SLIKLSTEQV QVNVIHKGVG
QISESDVTLA AASDAIIVGF QVRPSSSAGK LAEQEGVDIR KYSVIYDAIE EVKAAMEGML
APTLKEQITA TIEVREVFNI TKVGLVAGAM VKTGKVKRSD KARLIRDGIV VFTGAINALK
RFKDDVKEVG TNFECGISLT NCNDIKVGDI IEAYEEVEVK QTL
