ID   IF2_PROMM               Reviewed;        1125 AA.
AC   Q7V5M4;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PMT_1528;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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; BX548175; CAE21703.1; -; Genomic_DNA.
DR   RefSeq; WP_011130896.1; NC_005071.1.
DR   AlphaFoldDB; Q7V5M4; -.
DR   SMR; Q7V5M4; -.
DR   STRING; 74547.PMT_1528; -.
DR   EnsemblBacteria; CAE21703; CAE21703; PMT_1528.
DR   KEGG; pmt:PMT_1528; -.
DR   eggNOG; COG0532; Bacteria.
DR   eggNOG; COG3266; Bacteria.
DR   HOGENOM; CLU_006301_5_1_3; -.
DR   OMA; QVRPEMI; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000001423; 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..1125
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137234"
FT   DOMAIN          616..788
FT                   /note="tr-type G"
FT   REGION          32..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          625..632
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          650..654
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          675..678
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          729..732
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          765..767
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        129..145
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..235
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..453
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..511
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         625..632
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         675..679
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         729..732
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1125 AA;  119456 MW;  98F49A618173E0D5 CRC64;
     MTSSGKIRIY ELSKDLGLEN KDVLHAAEKL SIAAKSHSSS ISDDEAKRIR GLLRQGSAAN
     SAPPSKSEPE KTILSVKKAA PTAIKDVAPP IRKATSSSEI SHVKPSAPAN PIPTSPARPS
     TESVAHPAPP TRPANPTPTP TSSPPKTAAR PINAPISRPA IPSRPTAPTP RSANKPSSPV
     PPSAGGKDPR AGQTSTTSKA TTVSGGGPRP KIVSRPQSPT APGRSAPPAK PSIPSERKAP
     KPELVGRPKP KRPVVAPPSR PDPEGQRPDK KRPGISPRPI GGPNQRANTS QRPGAPIRQG
     KTRPGQPRSA GNTLELVGKP IRRDRSDAGS AGRDSNNRPG APTRPGMPTG MRKPVAPGEL
     MQLQKPTGRP GTPPPRRPDG TSVGTRGGSE GATPPVERTA TAPTAPKRPG HRPAQAPAAG
     APRRPGRPEW DDSAKLEALR NKSPQKQRQK VHIIGENDDA LTAETSGYAG EKQAVVLTAS
     LARPAKPKSQ KKPASKPVAA LRKRKKETTR QRQRRRAMEL RAAREAKQVR PEMLIVPEAN
     LTVQELADML SIESSEIIKS LFFKGITATV TQSLDLPTIE AVAEEFGVPV LQDDIEEAAK
     KTTEMIEETD LAHLIRRPPV VTVMGHVDHG KTSLLDAIRK ARVAAVEAGG ITQHIGAYQV
     EIDHGGQPRK ITFLDTPGHQ AFTAMRARGT KVTDIAVLVV AADDGVRPQT LEAISHARAA
     KVPIIVAINK TDKEGASPER VKQELSDQNL LSEEWGGDVV MVPVSAIKGE NIDKLLEMIL
     LVTEVEDLQA NPDRLAKGTV IEAHLDKAKG PVATLLIQNG TLKTGDVLAA GPVLGKVRAM
     VDDSGARLKE AGPSGAVEAL GFSEVPTAGD EFEVYPDEKS ARVVVGERAS DARATRLAQQ
     MASRRVSLAA MSGQASDGEL KELNLILKAD VQGSVEAILG SLEQLPKDEV QVRVLLSAPG
     EITETDVDLA AASGAVIVGF NTSMASGAKR AADATGVDVR DYDVIYKLLE DIQMAMEGLL
     EPELVEESLG EAEVRAVFTI GKSAVAGCYI TAGKLQRNCR VRVRRAKQVV FEGDLDSLRR
     NKDDVKEVAT GFECGIGCDR FANWEERDII EAHKLVTKRR TLSSS