IF2_MARMM
ID IF2_MARMM Reviewed; 861 AA.
AC Q0AK69;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Mmar10_3043;
OS Maricaulis maris (strain MCS10).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC Maricaulis.
OX NCBI_TaxID=394221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS10;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA Stephens C., Richardson P.;
RT "Complete sequence of Maricaulis maris MCS10.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000449; ABI67324.1; -; Genomic_DNA.
DR RefSeq; WP_011644968.1; NC_008347.1.
DR AlphaFoldDB; Q0AK69; -.
DR SMR; Q0AK69; -.
DR STRING; 394221.Mmar10_3043; -.
DR EnsemblBacteria; ABI67324; ABI67324; Mmar10_3043.
DR KEGG; mmr:Mmar10_3043; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001964; 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; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
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..861
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008268"
FT DOMAIN 357..527
FT /note="tr-type G"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..373
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 391..395
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 413..416
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 467..470
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 503..505
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 366..373
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 413..417
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 467..470
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 861 AA; 93250 MW; E1CA27EC3C746CA6 CRC64;
MSDADDNNSS GRRPLSLKRS GGGTVQQSFA RGRSKAVVVE KKRKRVATPA KDGGPGGKQG
GGAKGGESAL AAKARQLGLS EEELVARQRA IARARAEAAD REAQKKQDAA AMAQRAASEQ
RQLEEQRERV AREAREAEEA AQKAIEDEAR LKAEAEAATA AKDSGRKRDD ESSRRRPPAK
DEKRTPEVVP MDEASALEAL GGRVKRKGGA AGPGPAAKQQ PARAKTDNRR RGKLTIQNIL
EGDEERQRSL ASVRRARERE KQRRQDTSGG REKIEREVVV PEAITVADLA NRMAERSVDV
IKYMMKQGQM VRMNDVLDAD TAELVVEDFG HIVKRVSEAD VEQGFIDDDD ADEAKLPRAP
VIAVMGHVDH GKTSLLDALR STDIASGEAG GITQHIGAYQ VELKGGQKIT FLDTPGHAAF
SAMRSRGAMA TDIVILVVAA DDSVKPQTIE AIHHAKAAGT PIIVAVNKCD KHEANPQKVL
TDLLQHEIVV EAMSGEVQSV NVSAKTREGL DELTEAIALQ AELLDLKANP ERSAEGIVIE
SQVDKGRGPV ATLLVRRGTL KRGEIVVAGA QWGRVRALVD ARGQQLPEAG PSLAVEILGL
DGAPDPGELF AVVDSESRAR EIADYRQRKG REATGGSSPA SASLEQMMAR LKQDETQEMP
LLVKSDVQGS AEAIKQSLEG IGNDEVRARI IRAAPGGVNE SDVLLAKSSG APVFAFNVRA
NKQARELAER EGVEIRYYSV IYDVIDDVRN TMEGMLAPEK RENFIGYAEI LEVFNITKTG
KVAGCRVTEG VVRRGCGVRL LRDDTVLHEG KLKTLKRFKD EVSDVRAGTE CGMAFEKYED
LRKGDQIECF EVIEVARKLE A
