IF2_RHORT
ID IF2_RHORT Reviewed; 866 AA.
AC Q2RMS0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Rru_A3781;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
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 -!- SEQUENCE CAUTION:
CC Sequence=ABC24575.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000230; ABC24575.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_014626661.1; NC_007643.1.
DR RefSeq; YP_428862.1; NC_007643.1.
DR AlphaFoldDB; Q2RMS0; -.
DR SMR; Q2RMS0; -.
DR STRING; 269796.Rru_A3781; -.
DR EnsemblBacteria; ABC24575; ABC24575; Rru_A3781.
DR KEGG; rru:Rru_A3781; -.
DR PATRIC; fig|269796.9.peg.3903; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001929; Chromosome.
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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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; Reference proteome.
FT CHAIN 1..866
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335503"
FT DOMAIN 365..533
FT /note="tr-type G"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..381
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 399..403
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 421..424
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 475..478
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 511..513
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 374..381
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 421..425
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 475..478
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 866 AA; 93794 MW; 080CCECFA9A73506 CRC64;
MTNDKDRKAP LSLSPKGKLE LKKSAETGQV RQSFSHGRSK VVQVEVRKSK KRPATSGDPA
AVQNAIRGAA VFDTGLTSEE MQGRRRAVEE AVVRAAEEAE RKRLEEIERR RREEEEARLK
VEEEARRKAE EEAARAARAA AGDAAETPAE DVAPAAPQVA AAPQAPAPAP TRSGPRPGPD
ASARPAAEAP RSPTEAPRPG PRRVVEDEDD DAPKKVASRG AVPPKPAPAK RVEPKRRGKL
TVTAALEGDE RSERGRSVAA LRRAKQKEKR KAEMMSPAER VVREVIIPDV INVQELANRM
AERGANVIKT LMKMGVMATI NQTIDADTAE LVVAEFGHAS RRVSDSDVEL GLGDALPDGT
EVLTSRPPVV TVMGHVDHGK TSLLDAMRKT DVAGGEAGGI TQHIGAYQVV TKSGQKITFI
DTPGHAAFTA MRARGARVTD IVVLVVAAND GIMPQTIEAI RHARAAEVPV VVAINKMDLP
DANPEKVRTD LLQHELVVEQ LGGDVLNVEV SAKRRLNLDK LEEAILLQSE ILDLKANADR
ACQGVVIEAK VEKGRGSVAT ILVQKGTLKV GDIFVAGAEW GRVRALVDDH GNRVIAATPA
MPVEVLGFQG TPAAGDDFIV VEDENRAREI SEYRQRKDRD AQQVRTARGT MEQMFERIQA
GEARELPVVI KADVQGSVEA LVGTLEKLGN DDVKIRVLHA AVGAINESDV TLAKASDGLI
IGFNVRANPQ AREMARRDGI DIRYHSIIYA VADEVKALLS GMLEPTFKES FIGYAAIREV
FNITKVGKVA GCMVTEGIVK RGAKVRLLRD NVVIHEGSLS QLKRFKDDVR EVREGYECGM
SFETYNDIQV GDVIECFEME EVAAVL
