ID C3MC66_SINFN Unreviewed; 889 AA.
AC C3MC66;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100,
GN ECO:0000313|EMBL:ACP27291.1};
GN OrderedLocusNames=NGR_c35680 {ECO:0000313|EMBL:ACP27291.1};
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP27291.1, ECO:0000313|Proteomes:UP000001054};
RN [1] {ECO:0000313|EMBL:ACP27291.1, ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
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:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000645}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
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DR EMBL; CP001389; ACP27291.1; -; Genomic_DNA.
DR RefSeq; WP_012710036.1; NC_012587.1.
DR RefSeq; YP_002828044.1; NC_012587.1.
DR AlphaFoldDB; C3MC66; -.
DR STRING; 394.NGR_c35680; -.
DR KEGG; rhi:NGR_c35680; -.
DR PATRIC; fig|394.7.peg.6419; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000001054; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; 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; IPR004161; EFTu-like_2.
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 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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT DOMAIN 387..554
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..538
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 38..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 396..403
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 442..446
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 496..499
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 889 AA; 96445 MW; 28B6B3F9548AB577 CRC64;
MTDNKDDKTL SVAGKKTLTL KPSGVTQGTV RQDMGRGRTK AVVVETKKTR GLTRHKDERP
ITPVSAAPVA RPAEPRPVQP HPAGRPAPQP QPHQPRSEQN RPRIGVVLND LSAGEMEARR
RALADAQVRD AEEAKRRAEE EARRRVEEEA RLAREKEEAA RRAAEEAARP AVEVEKAEPA
VEAGRPLVAE RRTDTRPQPA RPASAAPQAP AAPAAALRGR RAGAEEEEER PRGGAGPARG
KVVRPEPAKP APRAKGDEGR RQGKLTLTAA VDEDGGQRGR SLSAMRRRQE KFRRSQMQET
REKISREVVL PETITIQELS QRMSERAVDV IKFLMKEGQM MKPGDLIDAD LAELIAGEFG
HTVKRVSESD VEEGIFNVAD SDETMVSRPP IVTIMGHVDH GKTSLLDAIR HANVVAGEAG
GITQHIGAYQ VEQNGQKITF IDTPGHAAFT AMRARGAQAT DIAVLVVAAD DSVMPQTIES
INHAKAAGVP IIVAINKIDK PTANPQKVRT ELLQHEVFVE SMGGEVLDVE VSAKNQTNLD
KLLEAILLQA EILDLKANPD RTAEGTVVEA ELDRGRGAVA TVLVQKGTLT PGQIIVAGDQ
WGRVRALVND KGEHVKEAGP SMPVEVLGLS GTPAAGDKFA VVENESRARE ISEYRQRLAR
EKMVARQSGS RGSLEQMMSQ LQASGLKEFP LVIKGDVQGS IEAIAGALDK LGTDEVRARI
VHSGAGGITE SDISLAEASN AAIIGFNVRA NKQARDAADR SGIEIRYYNI IYDLVDDVKA
AMSGLLSPER RETFLGNAEI LEVFNITKVG KVAGCRVTEG KVERGVGVRL VRDNVVIHEG
KLKTLKRFKD EVSEVQSGQE CGMAFENYED IRAGDTIECF RVEHITRTL
//
