IF2_PROM5
ID IF2_PROM5 Reviewed; 1161 AA.
AC A2BYM0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=P9515_16741;
OS Prochlorococcus marinus (strain MIT 9515).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167542;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9515;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000552; ABM72881.1; -; Genomic_DNA.
DR RefSeq; WP_011820974.1; NC_008817.1.
DR AlphaFoldDB; A2BYM0; -.
DR SMR; A2BYM0; -.
DR STRING; 167542.P9515_16741; -.
DR PRIDE; A2BYM0; -.
DR EnsemblBacteria; ABM72881; ABM72881; P9515_16741.
DR KEGG; pmc:P9515_16741; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_7_0_3; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001589; 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.
FT CHAIN 1..1161
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008299"
FT DOMAIN 653..830
FT /note="tr-type G"
FT REGION 67..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..669
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 687..691
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 712..715
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 766..769
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 802..804
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 67..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 662..669
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 712..716
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 766..769
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1161 AA; 127585 MW; E41C9E29522393CC CRC64;
MTISDKIRVY ELSRDLKLEN KDILDAAQKL SISVKSHSSS MSLEDAKKIK NLIRNGNSGK
KIISVSKSSF KAANEQQNNI DNQNKDSNSR SKPLNKEKPS KESLNKKPLL NKPVNKEENS
LISSNKKNTA KLKNPNPPSR ISNLQSQVLP NSHNKTQHTI KTKNPNEKKN STKIVQEKKS
LNNNSPLRTK SPARPPIQLI EKPKNLTTSN KDIKANKKND NSLNQRPQQA NRLNNNNNFP
KKNINNPRIK NTPELVGAPI RREDPKINSN RQNSNSRQPP SNIQASPNRP VIPNRQVTPN
RPSNPNRQGV SNRPGGGQNR QGVPNRPGSP YRPGNPNRQG MSNRPGVGGQ NRQGAPNRQG
SPYRQGDPNR QGGNYRQGDL NRSGSKFNNQ NPSGIRKPVA PNELMQLQKT NASDKEKLNR
SNFEKQKVEP PKQKAKAPNS RLNASPTAKK TPHRSFTNNS KKPGRSDWDD SAKLEALRNK
NPQKQRQKVH IIGENDDSLT SETSGYSGEK VSILSASLAR PKKEKSEEPK SQKTTRQFKK
KNKETTRQRQ KRRAMELRAA KDAKQVRPEM IIVPEDNLTV QELADKLSLE SSEIIKSLFF
KGITATVTQS LDLATIETVA EEFGVPVLQD DVEEAAKKTV DMIETDDIES LIKRPPVITV
MGHVDHGKTS LLDSIRESRV ASGEAGGITQ HIGAYQVEFE HESKKKKLTF LDTPGHEAFT
AMRARGTKVT DVAVLVVAAD DGCRPQTLEA ISHARAAKVP IVVAINKIDK EGASPDRVKQ
ELSEKDLIAE DWGGDVVMVP VSAIKKQNID KLLEMILLVS EVEDLQANPE RLAKGTVIEA
HLDKAKGPVA TLLVQNGTLK AGDVLAAGSV LGKIRAMVDE HGNRIKEAGP SCPVEALGFS
EVPTAGDEFE VYPDEKTARG IVGERATDAR ATKLAQQMAS RRVSLSSLST QANDGELKEL
NLILKADVQG SVEAILGSLE QLPKNEVQVR VLLSAPGEIT ETDIDLAAAS GSVIIGFNTS
LASGAKRAAD SNNVDIREYE VIYKLLEDIQ SAMEGLLEPD LVEESLGQAE VRATFAVGKG
AIAGCYIQSG KLQRNCSLRV LRSDKVIFEG NLDSLKRSKD DVKEVNTGFE CGVGCDKFST
WNEGDIIEAF KFVTKKRTLN K
