ID A0A1T5D4A4_9FIRM Unreviewed; 966 AA.
AC A0A1T5D4A4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN06296386_103281 {ECO:0000313|EMBL:SKB66588.1};
OS Lachnospiraceae bacterium.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1898203 {ECO:0000313|EMBL:SKB66588.1, ECO:0000313|Proteomes:UP000191179};
RN [1] {ECO:0000313|EMBL:SKB66588.1, ECO:0000313|Proteomes:UP000191179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1P17 {ECO:0000313|EMBL:SKB66588.1,
RC ECO:0000313|Proteomes:UP000191179};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC Rule:MF_00100, 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; FUZG01000003; SKB66588.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5D4A4; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000191179; Unassembled WGS sequence.
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; 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|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:UP000191179}.
FT DOMAIN 466..635
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 62..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..617
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 222..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 475..482
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 521..525
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 575..578
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 966 AA; 104349 MW; 6F37E82F6418D1A1 CRC64;
MAKMQILKLT KELKEKGISV SNKDVVEYLN ANGADVANHM SSIDDKYIDM VRSKFGGDAA
KKSDAAAKPA ADKTAEKAAG SAEGGDNKPK KKKHIIFATN NTGRGNRNNN GGRQIVKISN
GKIEQPKARK PFQHTEVASP DAFVGVKKEN VSAEKPAAAP APEKTEAPAP TVEKAAPAAV
NAAPEKTEEK PQTEAAKDNT TAEQSSPIKR VIGNVYANMA AMKKTTGNGN GNGSNNRSGN
GQGRGGNGNR PNNNNGQRRS FGQNNNQGGG QRGSFAQNGN RNFGNNNNRP GFNRSASRPG
SFNQNQNSRG GFAGGAAPAP AAGSGRGGAQ GHRYDADRRR QSEARRRKEA VAEASMEERA
RKKFNPHGFH KPAPVEKPVE EEIKVITIPD TLTIRELADH MKIQSAQIIK KLFLAGQVVT
LNSELSYDEA ENIAADYDIL CEHEKKVDVI AELLKEDEED ESVMSKRPPV VCVMGHVDHG
KTSLLDKIRQ TNVTDKESGG ITQAIGAYMV KIKDRKITFL DTPGHEAFTA MRMRGANSTD
IAVLVVAADD GVMPQTVEAI NHAKAAGVDI IVAVNKIDKP SANIDRVKQE LAEYELIPED
WGGSTVFVPV SAKSGEGIDT LLEMILLSAD MLELKANANR KARGLVIEAQ LDKGRGPVAS
VLVQKGTLHV GDFIAVGACH GRVRAMTDEN GKRIKEAGPS TPAEILGLDD VPEAGEIFIS
PNTDKEGKEF AETFKEQHKK ELLRETKQRM SLDDLYSQIK EGDLKEFNVI IKADVQGSVE
ALKQSLLKLS NDEVALKVIH GGVGAINESD VILASASNAV IIGFNVRPDA LAKQTAETEE
VDIHLYSVIY QAIDAVESAM KGLLAPVFEE KILGHVEIRQ IFKASQIGNI AGSYVTDGTV
ERGCSIRIKR DGELIHEGKL ASLKRFKDDV KEVREGYECG LVFEDFNDVK ELDVVECYKM
VEVARD
//
