IF2_BORBU
ID IF2_BORBU Reviewed; 882 AA.
AC O51741;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=BB_0801;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AE000783; AAC67153.1; -; Genomic_DNA.
DR PIR; H70199; H70199.
DR RefSeq; NP_212935.1; NC_001318.1.
DR RefSeq; WP_010889822.1; NC_001318.1.
DR AlphaFoldDB; O51741; -.
DR SMR; O51741; -.
DR STRING; 224326.BB_0801; -.
DR PRIDE; O51741; -.
DR EnsemblBacteria; AAC67153; AAC67153; BB_0801.
DR KEGG; bbu:BB_0801; -.
DR PATRIC; fig|224326.49.peg.1193; -.
DR HOGENOM; CLU_006301_1_1_12; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001807; 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; 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; 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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..882
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137174"
FT DOMAIN 380..553
FT /note="tr-type G"
FT REGION 38..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..396
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 414..418
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 435..438
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 489..492
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 525..527
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 244..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 389..396
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 435..439
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 489..492
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 882 AA; 97796 MW; 0FA20D65B5443C41 CRC64;
MSKNIDDIKN EDGKKVKIIK LKKKVVKIVT YNDLSVKNDS NSFVDLHNNS NKAEYSQSRD
NRTGGYSQNR DNRAGGYSQN RDNRAGGYSQ NRDNRTGGYS QNRDNRTGGY SQNRDNRTGG
YSQNRDNRGG YSQGRDNRTG GYSQSRDNRT GGYSQNRDNR TGGYSQNRDN RTGGYSQNRD
NRTGGYSQNR DSLSFQYQGS VKKTYVAKNN SQNKYTTTSM SFRRLIKTKV PAIVSSTPAA
DSENSKELNR KLGEKKKQQQ ESQKSYKRKK AETESKTIEQ KVFEQLQKKK RENLANPIPK
SIDIMGSITV SDLARKMNLK SSDLIAKLMA LGVMVTINEK IDSDTATILV EEYGSKVNVV
SIYDETVIEE EVEDQSKRVE KPPVITIMGH VDHGKTKLLS VLQNIDINQT ESGGITQHIG
AYTIVYNDRE ITFLDTPGHE AFTMMRSRGA QVTDIVVLVV SAIDGVMPQT IEAINHAKEA
NVPIIVAINK IDLPDSNPDK IKHQLSEYGL VSEDWGGDTI FVMISALKNI GISELLDMIL
LQSDMMLLKA NPSKRAIGKV LDAKIDLGRG IVCSVIIEDG TLYVGDSFVG GACYGKVKAL
ISEKGVSVKS VGPAKAISVL GFSSMPQAGD PFQVTKTEKE AKLISSKRQD LKKYESSKNV
KKVTMLNLYD SIKEGALKEL KIILKADVQG SVEALKNSLE KLTNDEVRVR VVHSSAGVIT
ETDISFASAS DAIVIGFHVR PTAKAQVLAD QEKVEIRKYN VIYDAINDVR SVLEGMLEPD
VEQQFIGFAE VRAVINVPKI GVIAGCYVSR GLIKRDAITN VMRDGLQIHS GKISSLKRFK
DDVKEVAEQY ECGIMIDNYA NIKEGDIIEA FEVKKVKKSF KT
