IF2_PROM1
ID IF2_PROM1 Reviewed; 1183 AA.
AC A2C4P1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, 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}; OrderedLocusNames=NATL1_18951;
OS Prochlorococcus marinus (strain NATL1A).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167555;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL1A;
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; CP000553; ABM76451.1; -; Genomic_DNA.
DR RefSeq; WP_011824428.1; NC_008819.1.
DR AlphaFoldDB; A2C4P1; -.
DR SMR; A2C4P1; -.
DR STRING; 167555.NATL1_18951; -.
DR EnsemblBacteria; ABM76451; ABM76451; NATL1_18951.
DR KEGG; pme:NATL1_18951; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_3; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000002592; 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..1183
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008297"
FT DOMAIN 675..847
FT /note="tr-type G"
FT REGION 55..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..691
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 709..713
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 734..737
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 788..791
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 824..826
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 55..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 684..691
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 734..738
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 788..791
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1183 AA; 128110 MW; 4BFE3ED5C9A1629D CRC64;
MTSSGKIRIY ELSKDLSLDN KDVLDAARKL AIAAKSHSSS ISTLEANQIK DFLKKSKTIN
STSKSSNKLD KQILSVKKNP VKTQKDQKTE PKKKNHDQTE LSQAKLNTLL KPSQTLIKNQ
DSSQANNQKA LKNKFPAQQQ ITAPSKPNKP LPPNPRVEVK PTISKPLTQA ESTIPQSEQK
KDGQFINQPK RSELAKKPTG QPQQINPQEP KRPLAPPSRP KIDIQDKKPL QPNNQKAKTR
INQGEISPQK VGQGNIQKIK SQNKQNQPSR TPQPPTKGNT LELVGAPIRR EKPVNKPHTN
EVRNKPVMPS RPGAPKPPAA ANRQGLSNRP GSNNKIGGTG RPGSQNRQGP NRGGVANRTT
QGQNRPGGNN RAGAPVRSGS PNRGGIQNRP GVPTRSLGGP NRSNNRPGVP SGMRKPVAPS
ELMQLQKPQA RPNAPQRKTD SPTSPRPKRE NSTGARPPVN RPTPAAPKKP AHRPGGTAAA
PRRTGRPDWD DSAKLDALRN KSPQKQRQKV HIIGENDDAL TAERGGFAGE QQAVVLSASL
ARPSKPKVGK RNNGKPLTAL KKRKKETTRQ RQRRRAMELR AAREAKLVRP EMIVVPEDNL
TVQELADMLS VESSEIIKSL FFKGITATVT QSLDLATIET VAEEFGVPVL QDDVEEAAKK
TVEMIEEGDL KYLIRRPPVV TVMGHVDHGK TSLLDAIRKS RVAAGEAGGI TQHIGAYQIE
TEHDGSTKKL TFLDTPGHEA FTAMRARGTR VTDVAILVVA ADDGVRPQTL EAISHARAAK
VPIVVAINKI DKEGSSPDRV KQELSEQDLL SEEWGGDVVM VPVSAIKSEN IDKLLEMVLL
VTEVEDLQAN PDRLAKGTVI EAHLDKAKGP VATLLVQNGT LKSGDVVAAG PVLGKVRAMV
DENGSRIKEA GPSCPVEALG FSEVPTAGDE FEVYPDEKAA RAVVGERATD ARAARLAQQM
ASRRVSLSSM SGQASEGELK ELNIILKADA QGSLEAILGS LEQLPKDEVQ VRVLLSAPGE
ITETDIDLAA ASGAVIVGFN TSMASGAKRA ADANGVDVRD YEVIYKLLED IQLAMEGLLE
PEMIEEALGV AEVRAIFSIG KSAVAGCYVT NGKIQRNCRA RVKRGKQIVF EGDLDSLKRN
KDDVKDVSTG FECGIGCDRF ANWEEGDQIE AFKLVTQRRK LTN
