IF2_BACSU
ID IF2_BACSU Reviewed; 716 AA.
AC P17889; O31757;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=BSU16630;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=2110148; DOI=10.1128/jb.172.5.2675-2687.1990;
RA Shazand K., Tucker J., Chiang R., Stansmore K., Sperling-Petersen H.U.,
RA Grunberg-Manago M., Rabinowitz J.C., Leighton T.;
RT "Isolation and molecular genetic characterization of the Bacillus subtilis
RT gene (infB) encoding protein synthesis initiation factor 2.";
RL J. Bacteriol. 172:2675-2687(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8491709; DOI=10.1128/jb.175.10.2880-2887.1993;
RA Shazand K., Tucker J., Grunberg-Manago M., Rabinowitz J.C., Leighton T.;
RT "Similar organization of the nusA-infB operon in Bacillus subtilis and
RT Escherichia coli.";
RL J. Bacteriol. 175:2880-2887(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Alpha;
CC IsoId=P17889-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P17889-2; Sequence=VSP_018753, VSP_018754;
CC -!- MISCELLANEOUS: [Isoform Beta]: The alternative initiation site Met-94
CC is uncertain. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; M34836; AAA22673.1; -; Genomic_DNA.
DR EMBL; Z18631; CAA79234.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13536.1; -; Genomic_DNA.
DR PIR; A35269; A35269.
DR RefSeq; NP_389545.1; NC_000964.3.
DR AlphaFoldDB; P17889; -.
DR SMR; P17889; -.
DR IntAct; P17889; 1.
DR MINT; P17889; -.
DR STRING; 224308.BSU16630; -.
DR jPOST; P17889; -.
DR PaxDb; P17889; -.
DR PRIDE; P17889; -.
DR EnsemblBacteria; CAB13536; CAB13536; BSU_16630.
DR GeneID; 939630; -.
DR KEGG; bsu:BSU16630; -.
DR PATRIC; fig|224308.43.peg.1758; -.
DR eggNOG; COG0532; Bacteria.
DR InParanoid; P17889; -.
DR BioCyc; BSUB:BSU16630-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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 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 Alternative initiation; Cytoplasm; GTP-binding; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..716
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000014461"
FT DOMAIN 217..386
FT /note="tr-type G"
FT REGION 50..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..233
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 251..255
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 272..275
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 326..329
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 362..364
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 64..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 226..233
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 272..276
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 326..329
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..93
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_018753"
FT VAR_SEQ 94
FT /note="V -> M (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_018754"
FT CONFLICT 56
FT /note="R -> A (in Ref. 3; CAB13536)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 78622 MW; 929877D99D295E11 CRC64;
MAKMRVYEYA KALNVSSKEI LTALKNMDLE VNNHMAMLEE KAIKKLDAKY KKGGARAKSQ
KPAETNKNKQ PQGVNQQSAG NQPNKIRDGK KNDVQNNQFN KNKKNNNNKK NKRNNNNNKN
QHQQKPVKPK KELPEKITFS GTLTVGALAE ELGKEPSELI KKLMLLGVMA TINQELDKDT
IELIASEYGV ETEEVIVLEE TELEKYEEPD NEEDLEIRPP VVTIMGHVDH GKTTLLDSIR
KTKVVEGEAG GITQHIGAYQ IEENGKKITF LDTPGHAAFT TMRARGAEVT DITILVVAAD
DGVMPQTVEA INHAKAAEVP IIVAVNKIDK ESANPDRVMQ ELTEYGLVPE AWGGETIFVP
LSALTGKGID ELVEMILLVS EVEELKANPN RQAKGTVIEA ELDKGRGSVA TLLVQTGTLH
VGDPIVVGNT FGRVRAMVND IGRRVKTAGP STPVEITGLN DVPQAGDQFL VFKDEKTARS
VGEARASKQL EEQRSDKAKL SLDDLFEQIK QGDVKDINLI VKADVQGSAE ALTAALQKIE
VEGVKVKIIH TGVGAITESD IILASASNAI VIGFNVRPDG NAKSTAEAEN VDIRLHRIIY
KVIDEIEAAM KGMLDPEYEE KVIGQVEVRQ TFKVSKIGTI AGGYVTEGTI TRDSGLRLIR
DGVVIFEGEV DVLKRFKDDV KEVSQGYECG ITIKKYNDIR EGDILEAFVM QEIERT
