ID W0U1Y7_9FIRM Unreviewed; 842 AA.
AC W0U1Y7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:CCO03799.1};
GN ORFNames=RBI_I00059 {ECO:0000313|EMBL:CCO03799.1};
OS Ruminococcus bicirculans (ex Wegman et al. 2014).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1160721 {ECO:0000313|EMBL:CCO03799.1, ECO:0000313|Proteomes:UP000027600};
RN [1] {ECO:0000313|EMBL:CCO03799.1, ECO:0000313|Proteomes:UP000027600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=80/3 {ECO:0000313|EMBL:CCO03799.1};
RX PubMed=23919528; DOI=10.1111/1462-2920.12217;
RA Wegmann U., Louis P., Goesmann A., Henrissat B., Duncan S.H., Flint H.J.;
RT "Complete genome of a new Firmicutes species belonging to the dominant
RT human colonic microbiota ('Ruminococcus bicirculans') reveals two
RT chromosomes and a selective capacity to utilize plant glucans.";
RL Environ. Microbiol. 16:2879-2890(2014).
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; HF545616; CCO03799.1; -; Genomic_DNA.
DR AlphaFoldDB; W0U1Y7; -.
DR STRING; 1160721.RBI_I00059; -.
DR KEGG; rus:RBI_I00059; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR Proteomes; UP000027600; Chromosome I.
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.
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 344..513
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 71..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..495
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 71..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 353..360
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 399..403
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 453..456
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 842 AA; 93119 MW; F20840A74E9D561D CRC64;
MSMKTTKYKL SDMAKDLKVT NNDLIECLGK LGGEPKKTQS VLTPDEISYV LEYYTQNNQV
DSFDAFYANN VKPVKEEKKA DKKPVKAEKK EKKAEKKPEP KPAPKAEAKP EPKPEPKAEP
KVEKKPEVKA ETKQPAPEQK KKQPAPQKPA KKKEHGVRQQ LGGFSDKKEA SGGYTISEDN
DSFGTQRTID TRGSYIELDK YNEKYDNLAN SKQNKSKDNF TKKQKLTQKS QQRKKQQFSH
KKETESEKLR RLELERARKQ QLKVMIPDEI VVSELASRLK VTATEVIKKL MGLGVMASIN
EVVDFDTAAL VAEELGAKVE KEVHVTIEER LIETDEDPEE SLQERCPVVV VMGHVDHGKT
SILDRIRNAH VTDTEAGGIT QHIGAYQVEY QGKKITFLDT PGHEAFTAMR ARGANVTDIA
ILVVAADDGI MPQTIESINH AKAAGVSIIV AINKMDKEGA DPDRVKQQLT EQSLVVEEWG
GDVIAVPVSA KTGMGIDELL ENILLVAEVK ELKANPDRLA RGTVVEARLD KGKGPVATLL
VQNGTLKSGD VIIAGTSVGR IRTMTNDKGR SIKEAGPSTP VEITGLGEVP SAGDVFNAVA
DEKLARELVE QRKHEAKEEQ FQQHQKVTLD NLFSQIAEGE MKELPIIVKA DVQGSVEAVK
QSLEKLSNDE VRVKVIHGGV GAVSESDVML ANASNAIIVG FNVRPDPVAK QNAEQSGVDI
RLYRIIYDAI EEITDAMKGM LAPKYREVET ARIEVRQVYK ISNVGTVAGS YVLDGKVGRN
NEIRVVRDGI VIAEDKMSSL KRFKDDAKEV AAGFECGITL EKFTDIKEGD IFEAFYMEEY
RD
//
