IF2_BARQU
ID IF2_BARQU Reviewed; 845 AA.
AC Q6G0P2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BQ02030;
OS Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Toulouse;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897700; CAF25706.1; -; Genomic_DNA.
DR RefSeq; WP_011179021.1; NC_005955.1.
DR AlphaFoldDB; Q6G0P2; -.
DR SMR; Q6G0P2; -.
DR STRING; 283165.BQ02030; -.
DR EnsemblBacteria; CAF25706; CAF25706; BQ02030.
DR KEGG; bqu:BQ02030; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000597; 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; 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 PANTHER; PTHR43381; PTHR43381; 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; 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.
FT CHAIN 1..845
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228171"
FT DOMAIN 343..512
FT /note="tr-type G"
FT REGION 45..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..359
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 377..381
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 398..401
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 452..455
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 488..490
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 45..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352..359
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 398..402
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 452..455
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 845 AA; 93498 MW; 68D50CF3410C5974 CRC64;
MSENNNDKIT VKKTLTLKRS VLETSTVKQN FSHGRTKAVV VETKRRKITR TDEKAETSQP
ITKPHVAPQR SKPRFEEAKP SESSMAKSNL SSAEMEARLR ALEEAHIQER ITREKVEEQA
RRIKEREESL RQAVQETEIH QEEQKEEKNP PVQTSPLSSA HSSIEPIDIA ITPKNITVTE
KRKADEIKND DRHSRRANPA KSEVRTPKVV KGANERRRGK LTLNSALDEE GSVRGRSMAA
MRRRQEKFKR AQNQEPKEKI SREVVIPETI TIQELAQRMA ERSVDVIKFL MKQEQMMKPG
DVIDADVAEL IAVEFGHTVK RVLESDVEEG IFNIADNPQK MQPRPPVVTI MGHVDHGKTS
LLDAIRKANV VSGEAGGITQ HIGAYQVEQN GQKITFIDTP GHAAFTAMRA RGARVTDIAV
LVVAADDSVM PQTVESINHA KAAGVPIIVA INKIDKPAAD AQKVRTELLQ HEVFVETMGG
ETLEVEVSAK TGQNLVKLLE AILLQAELLD LKADPKRTAE GVVIEAKLDR GRGSVATVLV
QKGTLHPSDI IVAGNEWGRV RALIDDHGRH VKEAVPSTPI EILGMQGTPQ AGDRFAVVTH
EAKAREIAEY RQRLARDKAV ARQTGSRSSL EQMMTKLQTT GIKEFPLIVK GDVQGSIEAI
ASALEKLGNE EVRARIVHSG AGGITESDIS LAEASNSAVI GFNVRANKQA CALAKTQGIE
IRYYNIIYDL VDDIKAAMSG LLSPEQRETF LGNAEILEVF NITKIGKVAG CRVIEGKIER
GAGVRLIRDN IVIHEGKLKT LKRFKDEVNE VQSGQECGIA FENYEDIRAG DTIEIFRIEH
INRTL
