ID A0A096B0K2_9BACT Unreviewed; 977 AA.
AC A0A096B0K2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=HMPREF2137_02535 {ECO:0000313|EMBL:KGF36342.1};
OS Hoylesella buccalis DNF00853.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=1401074 {ECO:0000313|EMBL:KGF36342.1, ECO:0000313|Proteomes:UP000029556};
RN [1] {ECO:0000313|EMBL:KGF36342.1, ECO:0000313|Proteomes:UP000029556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00853 {ECO:0000313|EMBL:KGF36342.1,
RC ECO:0000313|Proteomes:UP000029556};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC {ECO:0000256|ARBA:ARBA00003987}.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGF36342.1}.
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DR EMBL; JRNN01000028; KGF36342.1; -; Genomic_DNA.
DR RefSeq; WP_036871885.1; NZ_JRNN01000028.1.
DR AlphaFoldDB; A0A096B0K2; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000029556; 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; 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.
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}.
FT DOMAIN 476..646
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 63..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 485..492
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 532..536
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 586..589
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 977 AA; 108014 MW; 4A9E9F32976542FC CRC64;
MSIRLNKALR ELNIGLQTAV EFLEKKSELG EVKGEPSFKL SDAQYQALVE AFKQDAEVRN
QAEKIFQKKP KEKKRTSEAK EERVEEVVET ASSQQRYKPL GKIDLSVFDK KSAAKNADAQ
DDQKASESQE QPTKKAAAVS PEPKKDKVEK PAETPKAAPT VVEESKKDDQ KAEAMTESPT
VKKAQADKKQ KSDEHVESQE SDKPQERVEP QANDKPQEVD EKQESDEPQS GGDEIFQTKS
ELRLQNAPKV NVLGKIDLST INQSTRPKKK TKEERRKERE EKRGDGRKKR VRINQQRVDI
NAASRQIGNN GGGNANKSAY ADGRNANKKN RKGRGRNQKP LEVNEEEVAR QVKETLARLT
SKGTQNRKGA KYRKEKRDAI QERMTAEAKA ERKESKTLKL TEFVTVSELA TMMDIDVNKL
IGTLMSIGVM ASINQRLDAE TINLVADEFG FKTEYVSAEV QEAVAEEVDD ENDLLPRAPI
VTVMGHVDHG KTSLLDHIRN TNVIEGEAGG ITQHIGAYNV KLENGRYITF LDTPGHEAFT
AMRARGTQVT DIAIIIIAAD DSVMPTTKEA IAHAQAANVP MVFAINKIDK PGANPDKIRE
DLAQMNLLVE EWGGKYQCQE ISAKKGIGVN ELLEKVLLEA DMLDLKANPN RRATGSIIES
SLDKGRGYVS TVLVSNGTLR VGDDIIAGTS WGRIKAMFNV RNQRIESAEP AEPAIILGLN
GAPTAGDQFH VLETEQEVRD IANKRMQLQR EQGLRTQKRL TLSDISHRIA LGSFKELNII
VKGDTDGSIE ALSDSFIKMS TEKINVNVIF KSVGQISESD VTLADASDAI IVGFQVRPSA
SARKLAEQNG VEINTYSVIY DAIDDVRSAM EGMLDKVTKE VVTGEVEVKQ VYKISKVGTV
AGAMVTDGKV HRSDKARVVR DGIVVHTAPI NALKRYKDDV KEVATGFECG ISLVNFNDIQ
EGDIIETFTE IEVKQTL
//
