IF2_RHIME
ID IF2_RHIME Reviewed; 889 AA.
AC Q92SW4;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=R00239;
GN ORFNames=SMc02914;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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; AL591688; CAC41676.1; -; Genomic_DNA.
DR RefSeq; NP_384345.1; NC_003047.1.
DR RefSeq; WP_010968445.1; NC_003047.1.
DR AlphaFoldDB; Q92SW4; -.
DR SMR; Q92SW4; -.
DR STRING; 266834.SMc02914; -.
DR EnsemblBacteria; CAC41676; CAC41676; SMc02914.
DR GeneID; 61601718; -.
DR KEGG; sme:SMc02914; -.
DR PATRIC; fig|266834.11.peg.1605; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001976; 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..889
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137241"
FT DOMAIN 387..554
FT /note="tr-type G"
FT REGION 1..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..403
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 421..425
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 442..445
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 496..499
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 532..534
FT /note="G5"
FT /evidence="ECO:0000250"
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 218..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..261
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:0000255|HAMAP-Rule:MF_00100"
FT BINDING 442..446
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 496..499
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 889 AA; 96655 MW; 8A213FAED0BA34B5 CRC64;
MTDNKDDKTL SVAGKKTLTL KPSGVTQGTV RQDMGRGRTK AVVVETKRTR GPLKHKDERP
ITPVAATPAA RPAEQRPMPP QPSGRPAPQP QPHQPRQEQN RPRGGVVLND LSAGEMEARR
RALAEAQIRD AEEAKRRAED EVRRRREEEE RLAREKEEAA RRAAEEAARP PVEAEKTEEK
VEAASPAVGE RRAETRPQPG RAAPAATPAA PDGAALRGRR GTESEEDERR RSGAGAPRGK
VVRPEPAKPA PRAKGDEGRR QGKLTLTTAA VDEDGSQRGR SLSAMRRRQE KFKRSQMQET
REKISREVVL PETITIQELS QRMSERAVDV IKFLMKEGQM MKPGDLIDAD LAELIAGEFG
HTVKRVSESD VEEGIFNISD VDDDMQSRPP IVTIMGHVDH GKTSLLDAIR HANVVAGEAG
GITQHIGAYQ VEQNGQKITF IDTPGHAAFT AMRARGAQAT DIAVLVVAAD DSVMPQTIES
INHAKAAGVP IIVAINKIDK PSANPQKVRT ELLQHEVFVE SMGGEVLDVE VSAKNQTNLD
KLLEAILLQS EILDLKANPN RTAEGTVVEA ELDRGRGAVA TVLVQKGTLT PGQIIVAGDQ
WGRVRALVND KGEHVKAAGP STPVEVLGLS GTPAAGDRFA VVESESRARE ISEYRQRLAR
EKAVARQSGS RGSLEQMMTQ LQTSGVKEFP LVIKGDVQGS IEAISGALDK LGTDEVRARI
VHSGAGGITE SDVSLAEASN AAIIGFNVRA NKQARDASER AGIEIRYYNI IYDLVDDVKA
AMSGLLSPER RETFLGNAEI LEVFNITKVG KVAGCRVTEG KVERGVGVRL VRDNVVIHEG
KLKTLKRFKD EVSEVQSGQE CGMAFENYED IRAGDTIECF RVEHVTRTL
