IF2_BORAP
ID IF2_BORAP Reviewed; 782 AA.
AC Q0SM50; G0IRY3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=BAPKO_0854, BafPKo_0829;
OS Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=390236;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA Wilske B., Platzer M.;
RT "Comparative genome analysis: selection pressure on the Borrelia vls
RT cassettes is essential for infectivity.";
RL BMC Genomics 7:211-211(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=22123755; DOI=10.1128/jb.05951-11;
RA Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA Fraser-Liggett C.M., Schutzer S.E.;
RT "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT Lyme disease agent isolates.";
RL J. Bacteriol. 193:6995-6996(2011).
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; CP000395; ABH02078.1; -; Genomic_DNA.
DR EMBL; CP002933; AEL70018.1; -; Genomic_DNA.
DR RefSeq; WP_011601238.1; NC_008277.1.
DR AlphaFoldDB; Q0SM50; -.
DR SMR; Q0SM50; -.
DR STRING; 390236.BafPKo_0829; -.
DR PRIDE; Q0SM50; -.
DR EnsemblBacteria; AEL70018; AEL70018; BafPKo_0829.
DR KEGG; baf:BAPKO_0854; -.
DR KEGG; bafz:BafPKo_0829; -.
DR PATRIC; fig|390236.22.peg.790; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_1_1_12; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000005216; 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.
FT CHAIN 1..782
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008205"
FT DOMAIN 280..453
FT /note="tr-type G"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..296
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 314..318
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 335..338
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 389..392
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 425..427
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 289..296
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 335..339
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 389..392
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT CONFLICT 92
FT /note="D -> DGRTGGYSQNRDGRTGGYSQNRDGRTGGYSQNRD (in Ref. 2;
FT AEL70018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 782 AA; 86405 MW; D4E4D4BADE52A23B CRC64;
MSKNIDDKNE DGKKIKIIKL RKKVVKIVTH NDLSGKNNPS GSTDLHKHNN KVEYSHSRDG
RTGGYSQNRD GRTGGYSQNR DGRTGGYSQN RDSLTSQYQG STKKTYVAKN NTQNKYTTSV
SFRRVIKTKV PSIVSSASST DSENSKELNR KLGEKKKQQQ ESQKSYKRKK AETESKTIEQ
KVFEQLQKKK RENLANPIPK SIDIMGSITV SDLARKMNLK SSDLIAKLMA LGVMVTINEK
IDSDTATILV EEYGSKVNVV SIYDETVIEE EVEDQSKRIE KPPVITIMGH VDHGKTRLLS
VLQNIDINQT ESGGITQHIG AYTIVYNSRE ITFLDTPGHE AFTMMRSRGA QVTDIVVLVV
SAIDGVMPQT IEAINHAKEA NVPIIVAINK IDLPDSNPDK IKHQLSEYDL VPEDWGGDTI
FVLISALKNI GISELLDMIL LQADMMLLKA NPSKRAIGKV LDAKIDLGRG IVCSVIIEDG
TLYVGDSFVG GACYGKVKAL INDKGVSVKS VGPAKAISVL GFSSMPQAGD PFQVTKTEKE
AKLISSKRQD LKKYESSKNV KKVTMLNLYD SIKEGTLKEL KIILKADVQG SVEALKNSLE
KLTNDEVRVR VVHSSAGVIT ETDISFASAS DAIVIGFHVR PTVKAQILAD QEKVEIRKYN
VIYDAISDVK SVLEGMLEPD VEQQFIGFAE VRAVINVPKV GVIAGCYVSR GLIKRDAITN
VMRDGLQIHS GKISSLKRFK DDVKEVAEQY ECGIMIDNYA NIKEGDIIEA FEVKKVKKTF
KT
