IF2_CAUVC
ID IF2_CAUVC Reviewed; 1009 AA.
AC Q9AC25;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CC_0042;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK22030.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005673; AAK22030.1; ALT_INIT; Genomic_DNA.
DR PIR; B87254; B87254.
DR RefSeq; NP_418862.1; NC_002696.2.
DR RefSeq; WP_024265492.1; NC_002696.2.
DR AlphaFoldDB; Q9AC25; -.
DR SMR; Q9AC25; -.
DR STRING; 190650.CC_0042; -.
DR PRIDE; Q9AC25; -.
DR EnsemblBacteria; AAK22030; AAK22030; CC_0042.
DR KEGG; ccr:CC_0042; -.
DR PATRIC; fig|190650.5.peg.41; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000001816; 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..1009
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137186"
FT DOMAIN 505..675
FT /note="tr-type G"
FT REGION 1..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..521
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 539..543
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 561..564
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 615..618
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 651..653
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..181
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..324
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 514..521
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 561..565
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 615..618
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1009 AA; 107460 MW; E7322182DEFBFB6E CRC64;
MSDENENGRP GGRTPMTLKP RQGSVSAGVV KQSFSHGRTK TVVVETKRTR THAPASGNLA
APSSAERRHG EAPAPRPAPP QGGGGGSAGG LSQEELRARQ RVVDAAREAQ ARQVAEQAAA
EARARAAQEA AQREAAAKAA AERAAAAPPP VAQAPAAPAP AAPVTPPPAA PQAPRPVAQA
PVAPSAPRQD APRQDTRAAA PGQTRTYEPS RDRRDDRPST TTYRPAPQGD RPFNQRAPRP
DANANFGQRA PRPEGDRPRG PRPDGDRPQG DRGGYRGDRP QGDRPQGDRP QQTVRYSALA
PRPAPGARGP GGPPRGPRPG VPAAAPATPE IQRATRSAPR PGGGAMDRRP DEDDDRRKNA
APNKAVSRVK GAPQRREGRL TIQAVAGDGD SADRMRSLAS VRRAREREKE KRRGGAVEQA
RVAREVVIPD VITVQELSNR MAVRGVDIIK FLMRQGVMLK INDVIDNDTA ELVATEFGHT
VKRVSEADVE EGFIGADDHD EHMDLRPPVV TIMGHVDHGK TSLLDALRST DVAAGEAGGI
TQHIGAYQVR LKDGQRVTFL DTPGHAAFSS MRARGANITD IVVLVVAGDD GVMPQTIEAI
KHAKAAEVPI IVAVNKMDKP GSDPTRVVNE LLQHEIVVES LGGDTQLIEV SAKARTGLDN
LLEAILLQAE VLDLKANPDR SADGVVIEAK LDKGRGAVST VLVNRGTLKR GDIVVAGSQW
GKVRALLNER NEQLQEAGPA TPVEILGLDG VPSPGDAFAV VENEARAREL TEYRIRLKRE
KSMAPVGAGA SMADMMAKLQ DKKLKELPLV IKADVQGSAE AIIGSLDKMA TDEVRARIIL
SGAGAISESD VMLAKGAGAP VIGFNVRASA QARALAEREG VEIRYYAIIY DLLDDIKGVL
SGMLAPIQRE TFLGNAEVLQ AFDISKIGKV AGCKVTEGVV RKGAKVRIIR QDIVVLELGT
LQTLKRFKDE VNEVPVGQEC GMMFAGFQDI KVGDTIECFT VEEIKRQLD
