ID D8IC94_BRAP9 Unreviewed; 777 AA.
AC D8IC94;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100,
GN ECO:0000313|EMBL:ADK30767.1};
GN OrderedLocusNames=BP951000_0769 {ECO:0000313|EMBL:ADK30767.1};
OS Brachyspira pilosicoli (strain ATCC BAA-1826 / 95/1000).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=759914 {ECO:0000313|EMBL:ADK30767.1, ECO:0000313|Proteomes:UP000000332};
RN [1] {ECO:0000313|EMBL:ADK30767.1, ECO:0000313|Proteomes:UP000000332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1826 / 95/1000 {ECO:0000313|Proteomes:UP000000332};
RX PubMed=20625514; DOI=10.1371/journal.pone.0011455;
RA Wanchanthuek P., Bellgard M.I., La T., Ryan K., Moolhuijzen P., Chapman B.,
RA Black M., Schibeci D., Hunter A., Barrero R., Phillips N.D., Hampson D.J.;
RT "The complete genome sequence of the pathogenic intestinal spirochete
RT Brachyspira pilosicoli and comparison with other Brachyspira genomes.";
RL PLoS ONE 5:E11455-E11455(2010).
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:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000645}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
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DR EMBL; CP002025; ADK30767.1; -; Genomic_DNA.
DR AlphaFoldDB; D8IC94; -.
DR STRING; 759914.BP951000_0769; -.
DR KEGG; bpo:BP951000_0769; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_12; -.
DR InParanoid; D8IC94; -.
DR Proteomes; UP000000332; 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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR004161; EFTu-like_2.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000000332}.
FT DOMAIN 277..446
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..428
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 286..293
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 332..336
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 386..389
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 777 AA; 86117 MW; 902BACAB785A5610 CRC64;
MMPQINESND KNQQNLSSDN KPKKVIINKK SNNSNNTEES QASATVKKIK KVVVKKIIIH
NKTEKQDSAK TENVQTPEQR KPFNNNKFNN NRDNSNNNRE RDNKGFNKES NNRDFSRDKQ
YKNTQITPPP VEEVSFKKDN KKDNKKRDYE KKEKEYDKKS SQKDSKAEAA QRQENKIFNK
LQAKKLQQEQ RLASVEKEIS IMETITVGDL AKKMNLRASD IISKLMGMGT MARVNDIIDS
DTATIIADDF GCKVNVISLQ EEATIEIKED KPEDLKPRPP VVTIMGHVDH GKTSLLDAIR
HSNITSKESG GITQNIGAYK VKIPSGEIAF IDTPGHAAFT MMRARGAKST DIVILVVASD
DGVMPQTLEA LNHAKEANVP IIVAVNKMDL PNASMDKVKA ALSEHGLTPE EWGGDTQYIG
VSALTKQGIN DLLEAIILQA EMLELKANPN REAIGIVLEA SLDQGRGPVG TVLVQNGTLK
IGDYFVCGLS VGKVRAMVND LGQRVTKALP STPVEVLGFE KTPEAGESFN VMLDEKEAKA
IADKRVQLKQ QEALKANVKV TLENLYEKIA SDAMKEFKVI IKADVQGSAE ALRDALNKIQ
SDKIRFVSIY SASGAVTESD VNLAHASNAI IIAYRVRPSG KARELAEKLG IPIERYDIIY
EAIESIQNAM KGSLERLKKE VDIGTVEVRD VFHVPRVGTI AGCYVTSGKI ERNAGVRVMR
DNVLIYTSKI SSLRRVKDDV KEVATGYECG ASIENFNDIK KGDLLEIFKI EEITQEL
//
