IF2_BACP2
ID IF2_BACP2 Reviewed; 706 AA.
AC A8FDD1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BPUM_1566;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(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; CP000813; ABV62248.1; -; Genomic_DNA.
DR RefSeq; WP_012009993.1; NZ_VEIC01000002.1.
DR AlphaFoldDB; A8FDD1; -.
DR SMR; A8FDD1; -.
DR STRING; 315750.BPUM_1566; -.
DR PRIDE; A8FDD1; -.
DR EnsemblBacteria; ABV62248; ABV62248; BPUM_1566.
DR KEGG; bpu:BPUM_1566; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001355; 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; 2.
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..706
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000057651"
FT DOMAIN 207..376
FT /note="tr-type G"
FT REGION 55..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..223
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 241..245
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 262..265
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 316..319
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 352..354
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 55..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216..223
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 262..266
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 316..319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 706 AA; 77573 MW; F45B393091A9B93F CRC64;
MAKVRVYEYA KAIDVSSKDI IAALKDMNVE VNNHMATLED DTVKKLDAIY KKAKAKETAN
EKPAEQKKQS SNKINDRKKN DVQNNQFNKN KKNNNQNKNK NKRGGNNKSQ HQQARPVKPK
KELPEKIEFT NSMTVGQLAE ELGKETAEII KKLMMLGVMA TINQELDKDT VELIASEYGV
PVEEVIILEE TELEKYEVED KEEDMQVRPP VVTIMGHVDH GKTTLLDSIR KTKVVEGEAG
GITQHIGAYQ IEENGKKITF LDTPGHAAFT TMRARGAEVT DTTILVVAAD DGVMPQTVEA
INHAKAAEVP IIVAVNKIDK PTANPDRVMQ ELTEHGLVPE AWGGETIFVP LSAKTGEGID
ELIEMILLVS EVGELKANPN RAAKGTVIEA ELDKGRGSVA TLLVQTGTLH VGDPIVVGNT
FGRVRAMVND IGRRVKTAGP STPVEITGLN DVPNAGDQFL VFKDEKTARQ VGEARASKQL
DEQRSDKAKL SLDDLFEQIK QGEVKDINLI VKADVQGSAE ALTAALQKIE VEGVKVKIIH
TGVGAITESD IILASASNAI VIGFNVRPDG NAKSTAETEN VDIRLHRIIY KVIDEIEAAM
KGMLDPEYEE KVIGQVEVRQ TFKVSKIGTI AGGYVTEGTI TRDSGIRLIR DGVVIFEGEV
DVLKRFKDDV KEVSQGYECG ITIKKYNDIR EGDVMESFVM QEIERK
