ID A0A0E3UIU3_9BACT Unreviewed; 872 AA.
AC A0A0E3UIU3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 ORFNames=IMCC26134_10335 {ECO:0000313|EMBL:AKC83076.1};
OS Verrucomicrobia bacterium IMCC26134.
OC Bacteria; Verrucomicrobiota.
OX NCBI_TaxID=1637999 {ECO:0000313|EMBL:AKC83076.1, ECO:0000313|Proteomes:UP000033046};
RN [1] {ECO:0000313|EMBL:AKC83076.1, ECO:0000313|Proteomes:UP000033046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26134 {ECO:0000313|EMBL:AKC83076.1,
RC ECO:0000313|Proteomes:UP000033046};
RA Choi A., Kang I., Cho J.-C.;
RT "Complete genome sequence of Verrucomicrobia strain IMCC26134.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; CP011265; AKC83076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3UIU3; -.
DR STRING; 1637999.IMCC26134_10335; -.
DR KEGG; vba:IMCC26134_10335; -.
DR PATRIC; fig|1637999.3.peg.2226; -.
DR HOGENOM; CLU_006301_5_2_0; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000033046; 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; 1.10.10.2480; -; 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; 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; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR PRINTS; PR01217; PRICHEXTENSN.
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|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:UP000033046}.
FT DOMAIN 370..539
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 48..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..521
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 111..243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 379..386
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 425..429
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 479..482
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 872 AA; 90889 MW; C8750AD97E9CF327 CRC64;
MSIRVHELAK KLGMENKELI SLLKARNYDV KTSSSTVDNI SAEALEKEFE RPASAAPAPT
AAVTPPAAAA APEAAKPAAK GPAGMMVKSV GDVARERSEA AARATAEANP ATPAPPAPVQ
APAAPVAPPA PVSRPSAPPP LPVSAPPPIS RPPALPPVSR PASAPSVPSA PFGAPRPNAP
LVTPGLRPPA AAAAPSPASA PLRPPVSAPA SAPLQPPAFS RPAPAPAASP ASPPLPKPAA
YGAPKAPPAT ISAPGNPMLP VTPSAQTATI TDEGGVKIIH LKPPIIVRDF ATTLGMRPFK
LISELMEVGI FASINQSIDE AVAAKVAEKH GFLLEIKHRG EAAQQQVNPK EKEAARVKKQ
AEDEVVNMAV RPPVCCILGH VDHGKTSLLD AIRKANVASG EAGGITQHIG AYQIEHSGRK
ITFLDTPGHA AFNKMRARGA SVTDIAILVV AADDGFMPQT DEALKHAQTA AVTLMVAVNK
MDVKGANIER VKQQMQERNI APEDWGGETV TVPVSALKGT GLSDLLDMIL LQADVLELKA
NPKAEAAGII IESQVDVGRG PLATVLVQRG TLKVGDSLVC GAQWCKVRAM FNDKGESIKE
APPAAPVRVI GWSGAPDSGA QFKAVKNARE AENLAEEEAF ALKKVTASSD AAPKNVSVEQ
LFADIAATQG KTLKVIIKTD VFGSTEAVRH VLEGIKSSKV SLEVVSTDVG LIGKNDVLMA
GTGGAVIIGF NTKLENGVTP LAKHHGVRIE TFGIIYQLAD KVKEMMADLL DPDLKEIKLG
AAEVRATFPV GKGTVAGCLV TEGKITRNAN ARVRRKKDIV DEGKIDTLKR FKDDANEVRA
GLECGIRLGD FNGYEVGDVI EVYEIQKVRA SL
//
