ID IF2_CERS4 Reviewed; 836 AA.
AC Q3IYN5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RHOS4_27810;
GN ORFNames=RSP_1165;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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}.
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DR EMBL; CP000143; ABA80349.1; -; Genomic_DNA.
DR RefSeq; WP_011338758.1; NZ_CP030271.1.
DR RefSeq; YP_354250.1; NC_007493.2.
DR AlphaFoldDB; Q3IYN5; -.
DR SMR; Q3IYN5; -.
DR STRING; 272943.RSP_1165; -.
DR EnsemblBacteria; ABA80349; ABA80349; RSP_1165.
DR KEGG; rsp:RSP_1165; -.
DR PATRIC; fig|272943.9.peg.3144; -.
DR eggNOG; COG0532; Bacteria.
DR OrthoDB; 9811804at2; -.
DR PhylomeDB; Q3IYN5; -.
DR Proteomes; UP000002703; Chromosome 1.
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; 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 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; PF08364; IF2_assoc; 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; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..836
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228235"
FT DOMAIN 333..501
FT /note="tr-type G"
FT REGION 1..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..349
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 367..371
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 389..392
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 443..446
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 479..481
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 183..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 342..349
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 389..393
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 443..446
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 836 AA; 90924 MW; 4DFFDA9975CD9ED8 CRC64;
MSDTDGKKPL GLGGGSRSGQ VKQSFSHGRT KSVLVETKRK RVVVPKPGAS GSSTTTSSPS
HLGDPAKRPA GISDAEMERR LAALRAAKLR EVEDAKRRAD EERQREEERQ RRREELEAKE
REERERAEAL RQKAEDEERA RREAEEAARR AEEAKRAPAP AAPQPAPAES RASAPPSAKP
GLPPSRKERE READRDRTTK KDDSRRSGKL TLNEALSGEG GRTRSLAAMK RKQEKARQKA
MGFGHKAEKQ VRDVQLPETI LVQELANRMA ERAADVVKAL MKMGMMVTMN QSIDADTAEL
VIEEFGHRAV RVSDADVEHV IDTVEDKAED LQPRPPIITI MGHVDHGKTS LLDAIRKTSV
VSGEAGGITQ HIGAYQVKTE SGAVLTFLDT PGHAAFTSMR ARGAQVTDIV VLVVAADDAV
MPQTVEAIKH AKAAKVPMIV AINKIDKPDA DPNKVRTDLL QHEVIVEKMS GDVLDVEVSA
KTGLGLDELL ENIALQAEIL DLRANPSRQA QGAVIEAKLD VGRGPVATVL VQYGTLKRGD
IFVVGQQWGK VRALINDKGE RVDEAGPSVP VEVLGLNGTP EAGDVLNVVE TEAQAREIAD
YREKAARDKR AAAGAATTLE QLMAKAKADA DVAELPVVIK ADVQGSAEAI VQALEKVGND
EVRVRVLHYG VGAITETDIT LAEASQAAVI GFNVRANASA RQAANQKSVE IRYYSVIYDL
VDDVKKAASG LLKAEVREHF IGYAQIKEVF RITGVGNVAG CIVTEGVARR SAGVRLLRDN
IVIHEGTLKT LKRFKDEVKE VQSGQECGMA FERYEDIRPG DVIEIFEREE VQRKLA
//
