ID F3B992_9FIRM Unreviewed; 821 AA.
AC F3B992;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=HMPREF9477_00418 {ECO:0000313|EMBL:EGG84691.1};
OS Lachnospiraceae bacterium 2_1_46FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=742723 {ECO:0000313|EMBL:EGG84691.1, ECO:0000313|Proteomes:UP000018451};
RN [1] {ECO:0000313|EMBL:EGG84691.1, ECO:0000313|Proteomes:UP000018451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_1_46FAA {ECO:0000313|EMBL:EGG84691.1,
RC ECO:0000313|Proteomes:UP000018451};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Ambrose C., Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 2_1_46FAA.";
RL Submitted (DEC-2012) 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}.
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:EGG84691.1}.
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DR EMBL; ADLB02000007; EGG84691.1; -; Genomic_DNA.
DR AlphaFoldDB; F3B992; -.
DR STRING; 742723.HMPREF9477_00418; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000018451; 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; 2.
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:UP000018451}.
FT DOMAIN 322..491
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 49..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..473
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 69..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 331..338
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 377..381
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 431..434
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 821 AA; 90967 MW; 3DF6333C878CF029 CRC64;
MSKIRVHELA KELNKTNKEL LDFLKSKEIG VKSHMSSLSD EQIQMVKGAM AGKATKTDGE
DAQKKKNIVQ VFRPQNSKQN NRPKQNNHKQ NQNQNNNNNQ GNTKQMNNGQ NNPRQNNNQG
KRQNNNQGGR YQNNNQNGER KNNNQSGRPN KNFNNSQRRD DRRDDNRRND KRTPSIPAPV
LPEQKPQRQK AKDKDAYKKK DYRQDDREDR KVKQTKKGKP APQPQKPQPK AEQKVEEKIS
MITIPEVLTI KELADKMKIQ PSAIVKKLFM QGKIVTVNQE VDFETAEEIA MEFEVLCEKE
EVVDVIEELL KEDEEDETTM EKRPPVVCVM GHVDHGKTSL LDAIRNTNVI DREAGGITQH
IGAYVANVNG ERITFLDTPG HEAFTAMRLR GAQSTDIAIL VVAADDGVMP QTVEAISHAK
AAGIEIIVAV NKIDKPSANI ERVKQELTEY ELIPEDWGGS TIFVPVSAKT GEGLEDLMEM
ILLTAEVLEL KANPNRQARG LVIEAELDKG KGSVATVLVQ KGTLRVGDAI AAGSAHGRVR
AMIDDKGRRV KEAGPSTPVE ILGLNDVPNA GEVFVGCAND KEARSFAETF ISQGRVKMLE
ETKSKMSLDD LFTQIQAGNL KELGIIVKAD VQGSVEAVKQ SLVKLSNDEV VIKIIHGGVG
AINESDVTLA SASNAIIIGF NVRPDATAKE IAEREGVDLR LYRVIYNAIE DVEAAMKGML
DPVFEEKVLG HAEVRQTFKA SGVGTIAGSY VLDGVFERNC SARVVRDGVV IFDGALASLK
RFKDDVKEVK AGYECGFVFE KFNDVKEGDQ VEAYKMVEIP R
//
