IF2_CERS5
ID IF2_CERS5 Reviewed; 838 AA.
AC A4WW80;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=Rsph17025_2757;
OS Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=349102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17025 / ATH 2.4.3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL Submitted (APR-2007) 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:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00100}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000661; ABP71644.1; -; Genomic_DNA.
DR AlphaFoldDB; A4WW80; -.
DR SMR; A4WW80; -.
DR STRING; 349102.Rsph17025_2757; -.
DR PRIDE; A4WW80; -.
DR EnsemblBacteria; ABP71644; ABP71644; Rsph17025_2757.
DR KEGG; rsq:Rsph17025_2757; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; RSPH349102:G1G8M-2837-MON; -.
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; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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 PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..838
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008319"
FT DOMAIN 335..509
FT /note="tr-type G"
FT REGION 1..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..351
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 369..373
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 391..394
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 445..448
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 481..483
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 344..351
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 391..395
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 445..448
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 838 AA; 90964 MW; F71B949C837CFEE8 CRC64;
MSDTDGKKPL GLGGGSRSGQ VKQSFSHGRT KSVLVETKRK RVVVPKPGAS GSSTTTSSPS
HLGDPAKRPA GISDAEMERR LAALRAAKLR EVDDAKRRAE EERQREEERQ RRREELEAKE
REERERAEAL RQKAEDEERA RREAEEAARR AEEAKRAPAP APAAAQPDAA DSRASAPTSA
KPGLPPSRKE REREADRDRT TKKDDSRRSG KLTLNEALSG EGGRTRSLAA MKREQEKARQ
KAMGFGHKAE KQVRDVQLPE TIVVQELANR MAERAADVVK ALMKMGMMVT MNQSIDADTA
ELVIEEFGHR AVRVSDADVE HVIDTVEDKA EDLQPRPPII TIMGHVDHGK TSLLDAIRKT
SVVSGEAGGI TQHIGAYQVK TESGAVLTFL DTPGHAAFTS MRARGAQVTD IVVLVVAADD
AVMPQTVEAI KHAKAAKVPM IVAINKIDKP DADPNKVRTD LLQHEVIVEK MSGDVLDVEV
SAKTGLGLDE LLENIALQAE LLDLRANPKR AAQGAVIEAK LDVGRGPVAT VLVQHGTLKR
GDIFVVGQQW GKVRALVNDK GERVDEAGPS VPVEVLGLNG TPEAGDVLNV VETEAQAREI
ADYREKAARD KRAAAGAATT LEQLMAKAKA DADVAELPVV IKADVQGSAE AIVQALEKVG
NEEVRVRVLH YGVGAITETD IGLAEASQAA VIGFNVRANA SARQAANQKS VEIRYYSVIY
DLVDDVKKAA SGLLKAEVRE HFIGYARIQE VFRITGVGNV AGCLVTEGVA RRSAGVRLLR
DNVVIHEGTL KTLKRFKDEV KEVQSGQECG MAFERYEDIR AGDVIEIFER EEVERKLA
