IF2_GLOC7
ID IF2_GLOC7 Reviewed; 1101 AA.
AC B7KIU2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=PCC7424_2357;
OS Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC
OS 7424)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Gloeothece; Gloeothece citriformis.
OX NCBI_TaxID=65393;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7424;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(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}.
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DR EMBL; CP001291; ACK70778.1; -; Genomic_DNA.
DR RefSeq; WP_015954382.1; NC_011729.1.
DR AlphaFoldDB; B7KIU2; -.
DR SMR; B7KIU2; -.
DR STRING; 65393.PCC7424_2357; -.
DR PRIDE; B7KIU2; -.
DR EnsemblBacteria; ACK70778; ACK70778; PCC7424_2357.
DR KEGG; cyc:PCC7424_2357; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_7_0_3; -.
DR OMA; NIAVKSH; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002384; 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.
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..1101
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000190630"
FT DOMAIN 592..765
FT /note="tr-type G"
FT REGION 81..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..608
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 626..630
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 651..654
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 705..708
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 741..743
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 109..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..376
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 601..608
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 651..655
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 705..708
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1101 AA; 121652 MW; 8CC5E2BCD62F954A CRC64;
MSNSKVRIYE LSKELNLDNK DILEICDQLN IAVKSHSSTI TESQAERIKA KAEKLNHQMA
GKIHSGSGID RGQNLAKERK QEILAIHHKP NRPFSSTDAP VGSGQSSPLI EPPRPPMKPQ
PPSPSRSEVT SPITDEPVST QEDTNGSSSS HEREPQSPMS PFDQQQPEQN TTDHNQEQQN
QLKYNQEQSN QLEQESAISS ELSEVNVSKL LRPPVRPSEK PASVPSPSKE KEAKSNEPTK
AQPIISPKEN KSHSKENKLK LPSDIKPKPN KDKDRDGKKP DKEKDKKSLS PQPKVKRESR
EQREPRESRE QREPRESREQ REPRESREQR EPKLSTELKR PTPPKPPQKP KQAEVAALAI
EPEDVEDTAE DLLEEDPLEA LTQKPKLKRP TPPKVGKRQN WDEEEEETEE GKGKAGKAAK
AGKNKRRQLL LEDEDDFDSD LEEILEIPTA VSISTARPPK PKSMKPAASG NGASKNVKAP
TKAEPGRGKS AERERSERKD RKEQPQRAET LVLDKTMTVR ELAERLGIAE TEIIRILFFK
GIAVNITQTL DFDTIQAIAE ELEVQIESPE VKAAATKTTE MLDANDLENL HRRPPVVTIM
GHVDHGKTTL LDSIRKTKVA QGEAGGITQH IGAYHVDIEH EGKQEQIVFL DTPGHEAFTA
MRARGARVTD IAILVVAADD GVQPQTREAI SHARAAEVPI VVAINKIDKP ESNPDRIKQE
LSELSLVPEE WGGETIMVPV SALKGENLDT LLEMLLLVAE VGELSANPDR LARGTVIEAN
LDRTRGPVAT LLVQNGTLRV GDTIVAGPVL GKIRAMIDDR GNKVEEASPS FAVEILGLNE
VPAAGDEFEV FENEKEARAL ADQRSQDLRQ TRLQQAMSSR RISLSTLSAQ AQEGKLKELN
LILKADVQGS VEAILGSLKQ LPQNEVQIRV LLAAPGEITE TDVDLAAASG AVIVGFNTTL
ASGARQSADQ EGIDIREYNI IYKLLDDIQG AMEGLLDPEE VESPLGVAEV RAVFPVGRGA
VAGCYVQSGK IIRNRQLRVR RKGEVIYEGV LDSLKRMKED AREVNAGYEC GIGVSKFNDW
QEGDSIEVFE MVMKRRTLST K
