IF2_SYNP2
ID IF2_SYNP2 Reviewed; 979 AA.
AC B1XI09;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=SYNPCC7002_A0755;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) 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; CP000951; ACA98760.1; -; Genomic_DNA.
DR RefSeq; WP_012306384.1; NC_010475.1.
DR AlphaFoldDB; B1XI09; -.
DR SMR; B1XI09; -.
DR STRING; 32049.SYNPCC7002_A0755; -.
DR EnsemblBacteria; ACA98760; ACA98760; SYNPCC7002_A0755.
DR KEGG; syp:SYNPCC7002_A0755; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_7_0_3; -.
DR OMA; NIAVKSH; -.
DR Proteomes; UP000001688; 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; 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; PF04760; IF2_N; 2.
DR PRINTS; PR00315; ELONGATNFCT.
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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..979
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093835"
FT DOMAIN 468..641
FT /note="tr-type G"
FT REGION 33..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..484
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 502..506
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 527..530
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 581..584
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 617..619
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 75..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..172
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 477..484
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 527..531
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 581..584
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 979 AA; 105721 MW; 752F2DD9F12CA721 CRC64;
MNNEKVRIYE LSKELDLENK DILEFCGQLS IDVKSHSSTI TTEEADKIRA IATQKRPQAP
KAQRPQRKKK QEILSVQHQP QGAKPQASKS ESADANHPTS TAKKLERPKL QSPPSRGKET
PAQPEESPAN NGAKAEPVAK TTSPKAEPAA PAAPKPKLMG PPPRPTPKSS APKTPDASPA
TAETSSGATQ ADVRAKSLSK NTAEAPAKAP KLRPKPQIVG TVSKKPTPVQ AIEPELDEEP
DTNNVEGDDD ATPEVLLAPP KRPAAKPKKA IGPKPSKRKV WEDEEEDESE SKKTKTSKLK
RRPVVIDDDD DDFGTTTNNN AEVPSVSLSI ARPPKPKSAS SSPSPSKPSP SKPKKPAAKR
SGSGGSGQSQ KEQRRDRPDV KTPPAEITLT ETMTLREMAD ILCIAETDII RRLFSKGIAI
NITQTLDYDT AQMVAEEFDV KVIAPEVKSA AEKSTEMLDV ADLEHLQHRP PVVTIMGHVD
HGKTTLLDSI RETKVAQGEA GGITQHIGAY HVDIEHNGKP GQIVFLDTPG HEAFTAMRAR
GAKVTDIAIL VVAADDGVRP QTLEAIRHAQ AAKVPIVVAI NKMDKLGAEP DRVKQELSEQ
GLVPEEWGGE TIMVPVSALK GENLDTLLEM ILLVSEIEEL SANPDRLARG TIIEAHLDRA
RGPVATLLVQ NGTLRVGDII VAGSVMGKIR AMISDRGEKV TDATPSFAVE ILGLSEVPAA
GDEFEVYSSE KEARAIADER AEGKRQSRLQ QAMSSRRVSL SSLSAQAQEG ELKELNLVLK
ADVQGSVEAI LGSLQQLPQD EVQIRVLLSA PGEISETDVD LAAASGAIII GFNTTLAPGA
RQAAEQEGVD IREYNVIYRF LEEIQGAMEG LLDPEEVEEP LGRAEVRAVF PVGRGSVAGC
YVQSGKVVRN RMIRVRRGDV VVYDGSLDSL KRVREDVREV NSGYECGIGV DKFSTWKEGD
IIEAYEMVFK RRTLAGRTS
