IF2_XANCB
ID IF2_XANCB Reviewed; 916 AA.
AC B0RRB4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=xcc-b100_1649;
OS Xanthomonas campestris pv. campestris (strain B100).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=509169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B100;
RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA Puehler A.;
RT "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT the reconstruction of metabolic pathways involved in xanthan
RT biosynthesis.";
RL J. Biotechnol. 134:33-45(2008).
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; AM920689; CAP50999.1; -; Genomic_DNA.
DR AlphaFoldDB; B0RRB4; -.
DR SMR; B0RRB4; -.
DR KEGG; xca:xcc-b100_1649; -.
DR HOGENOM; CLU_006301_6_0_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001188; 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; IPR009061; DNA-bd_dom_put_sf.
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; SSF46955; SSF46955; 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..916
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335520"
FT DOMAIN 415..584
FT /note="tr-type G"
FT REGION 151..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..431
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 449..453
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 470..473
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 524..527
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 560..562
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 153..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 424..431
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 470..474
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 524..527
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 916 AA; 97592 MW; EA50572C92F3FA1F CRC64;
MLWARGRQPD HRIRMSQQTT IRKLAELVNT PVDKLLVQLA EAGMKFSGPD QVVTSTEKMK
LLGFLRRTHG KADTPAEAAS EAAKKITLNR RKLQEVTVNA GRTKTTVNVE VRQKRTYVKS
DNEGSGRAAP MTPDEERADI LAKLAASRQR NLDEQQRLAE SDRARDEAIQ RKRDEEQAAK
DRVEAERKAA EEAAAAASAP APVAAAPAPS SAPAARAPSS PSSAPRPARP AGASPASRPA
TPARPDDRNN AAKHKTRGSH VMVAGVEDDD ATKRFAGQLH LSAADRARRS NVRGKPTGRP
GSSSSRRNDG GRGSNQSNSG PHGFERPTAP VVREVAIGET ITVADLAQKL ALKGGDVVKA
LFKMGVMATI TQSIDHDTAA LVTEELGHKA VRADNADFED ALLAHAEDAQ GETTSRPPVV
TIMGHVDHGK TSLLDYIRRT KIASGEAGGI TQHIGAYHVE TGRGVISFLD TPGHAAFTSM
RARGAKITDI VVLVVAADDG VMPQTKEAVA HAKAAGVPLI VAVNKIDKAG ADPLRVKNEL
LAENVVAEDF GGDTQFIEVS AKVGTGVDTL LDAISLQAEV LELKAVADGR ASGTVIESSL
DKGRGPVATV LVQQGALKRG DYLVCGIQYG RVRALFDETG HQPASAGPSI PVQVLGLSGV
PEAGDDFVVV DDERLAKDVA QQRETKRRES RLVASATNRM EDILAQMGKG EGQQVLNLVI
KADVQGSVEA LKQSLVALSN DDIRINVIHS GVGGITESDA NSAAASKATI IGFNVRADAS
ARKIVESNGI DLRYFSIIYD VIDQVKQVAS GLLGVEIREE IIGIAQVRDV FRSSKFGAVA
GCMIIEGVVK RSKPIRVLRD SVVVFEGELE SLRRFKENVD EVRNGTECGI GVKAYNDVKA
GDQIECFERI EVARTL
