ID IF2_XANC5 Reviewed; 904 AA.
AC Q3BRP5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=XCV2837;
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10;
RX PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT genome sequence.";
RL J. Bacteriol. 187:7254-7266(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}.
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DR EMBL; AM039952; CAJ24516.1; -; Genomic_DNA.
DR RefSeq; WP_011347934.1; NZ_CP017190.1.
DR AlphaFoldDB; Q3BRP5; -.
DR SMR; Q3BRP5; -.
DR STRING; 456327.BJD11_08690; -.
DR KEGG; xcv:XCV2837; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR Proteomes; UP000007069; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 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; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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..904
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228262"
FT DOMAIN 403..572
FT /note="tr-type G"
FT REGION 103..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..419
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 437..441
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 458..461
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 512..515
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 548..550
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 137..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 412..419
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 458..462
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 512..515
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 904 AA; 96171 MW; 19BD2488FBB66D66 CRC64;
MSQQTTIRKL AELVNTPVDK LLVQLAEAGM KFSGPDQVVT STEKMKLLGF LRRTHGKAET
SAEAASEAAK KITLNRRKLQ EVTVNAGRTK TTVNVEVRQK RTYVKSENEG SGRAAPMTPD
EERADILRKL EESRQRNLEE QQRLAESDRV RDEAIQRKRE EEQAAKDRAE AERKAAEEAA
AAASAPAPVA DAPTPSAAAP AARSPSSPSS APRAARPAGA SPASRPAAPA RADDRSNAAK
HKTRGSHVMV AGVEDDDATK RFAGQLHLSA ADRARRSNVR GKPTGRPGSS SSRRGNDNGR
GGSQANSGPH GFERPTAPVV REVAIGETIT VADLAQKLAL KGGDVVKALF KMGVMATITQ
SIDHDTAALV TEELGHKAVR ADNADFEDAL LAHAEDAQGE ATSRPPVVTI MGHVDHGKTS
LLDYIRRTKI ASGEAGGITQ HIGAYHVETG RGVISFLDTP GHAAFTSMRA RGAKITDIVV
LVVAADDGVM PQTKEAVAHA KAAGVPLIVA VNKIDKTGAD PLRVKNELLA ENVVAEEFGG
DTQFIEVSAK VGTGVDTLLD AISLQAEVLE LKAVAEGRAS GTVIESSLDK GRGPVATVLV
QQGALKRGDY LVCGIQYGRV RALFDETGHQ PASAGPSIPV QVLGLSGVPE AGDDFVVVDD
ERLAKDVAQQ RETKRRESRL VASATNRMED ILAQMGKGEG QQVLNLVIKA DVQGSVEALK
QSLVALSNED IRINVIHSGV GGITESDANS AAASKATIIG FNVRADASAR KIVESNGIDL
RYFSIIYDVI DQVKQVASGL LGVEIREEII GIAQVRDVFR SSKFGAVAGC MVIEGVVKRS
KPIRVLRDSV VVFEGELESL RRFKENVDEV RNGTECGIGV KAYNDVKAGD QIECFERIEV
ARTL
//
