IF2_XANC8
ID IF2_XANC8 Reviewed; 902 AA.
AC Q4UWA2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=XC_1605;
OS Xanthomonas campestris pv. campestris (strain 8004).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=314565;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8004;
RX PubMed=15899963; DOI=10.1101/gr.3378705;
RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT "Comparative and functional genomic analyses of the pathogenicity of
RT phytopathogen Xanthomonas campestris pv. campestris.";
RL Genome Res. 15:757-767(2005).
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=AAY48671.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000050; AAY48671.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_019237528.1; NC_007086.1.
DR AlphaFoldDB; Q4UWA2; -.
DR SMR; Q4UWA2; -.
DR EnsemblBacteria; AAY48671; AAY48671; XC_1605.
DR KEGG; xcb:XC_1605; -.
DR HOGENOM; CLU_006301_6_0_6; -.
DR Proteomes; UP000000420; 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..902
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228261"
FT DOMAIN 401..570
FT /note="tr-type G"
FT REGION 137..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..417
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 435..439
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 456..459
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 510..513
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 546..548
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 139..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 410..417
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 456..460
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 510..513
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 902 AA; 95832 MW; 507A00B4AC95EBBE CRC64;
MSQQTTIRKL AELVNTPVDK LLVQLAEAGM KFSGPDQVVT STEKMKLLGF LRRTHGKADT
PAEAASEAAK KITLNRRKLQ EVTVNAGRTK TTVNVEVRQK RTYVKSENEG SGRAAPMTPD
EERADILAKL AASRQRNLDE QQRLAESDRA RDEAIQRKRD EEQAAKDRVE AERKAAEEAA
AAASAPAPVA AAPAPSSAPA ARAPSSPSSA PRPARPAGAS PASRPATPAR PDDRNNAAKH
KTRGSHVMVA GVEDDDATKR FAGQLHLSAA DRARRSNVRG KPTGRPGSSS SRRNDGGRGS
NQSNSGPHGF ERPTAPVVRE VAIGETITVA DLAQKLALKG GDVVKALFKM GVMATITQSI
DHDTAALVTE ELGHKAVRAD NADFEDALLA HAEDAQGETT SRPPVVTIMG HVDHGKTSLL
DYIRRTKIAS GEAGGITQHI GAYHVETGRG VISFLDTPGH AAFTSMRARG AKITDIVVLV
VAADDGVMPQ TKEAVAHAKA AGVPLIVAVN KIDKAGADPL RVKNELLAEN VVAEDFGGDT
QFIEVSAKVG TGVDTLLDAI SLQAEVLELK AVADGRASGT VIESSLDKGR GPVATVLVQQ
GALKRGDYLV CGIQYGRVRA LFDETGHQPA SAGPSIPVQV LGLSGVPEAG DDFVVVDDER
LAKDVAQQRE TKRRESRLVA SATNRMEDIL AQMGKGEGQQ VLNLVIKADV QGSVEALKQS
LVALSNDDIR INVIHSGVGG ITESDANSAA ASKATIIGFN VRADASARKI VESNGIDLRY
FSIIYDVIDQ VKQVASGLLG VEIREEIIGI AQVRDVFRSS KFGAVAGCMI IEGVVKRSKP
IRVLRDSVVV FEGELESLRR FKENVDEVRN GTECGIGVKA YNDVKAGDQI ECFERIEVAR
TL
