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 27-MAR-2024, entry version 125.
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; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; 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 KEGG; pmt:PMT_1528; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR HOGENOM; CLU_006301_5_1_3; -.
DR OrthoDB; 9811804at2; -.
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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 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; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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
//
