ID   IF2_XANAC               Reviewed;         904 AA.
AC   Q8PJ55;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=XAC2687;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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; AE008923; AAM37534.1; -; Genomic_DNA.
DR   RefSeq; WP_011051766.1; NC_003919.1.
DR   AlphaFoldDB; Q8PJ55; -.
DR   SMR; Q8PJ55; -.
DR   STRING; 190486.XAC2687; -.
DR   PRIDE; Q8PJ55; -.
DR   EnsemblBacteria; AAM37534; AAM37534; XAC2687.
DR   GeneID; 66911776; -.
DR   KEGG; xac:XAC2687; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_3_6; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000000576; 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..904
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137285"
FT   DOMAIN          403..572
FT                   /note="tr-type G"
FT   REGION          102..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..316
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        134..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;  96181 MW;  BB292B856F63B3BE CRC64;
     MSQQTTIRKL AELVNTPVDK LLVQLAEAGM KFSGPDQVVT STEKMKLLGF LRRTHGKAET
     SAEAASEAAK KITLNRRKLQ EVTVNAGRTK TTVNVEVRQK RTYVKSENEG GGRAAPMTPD
     EERADILRKL EESRQRNLEE QQRLAESDRV RDEAIQRKRE EEQAAKDRAE AERKAAEEAA
     AAASAPAPVA DAPKPSAAAP AARLPSSPSS APRAARPAGA SPASRPAAPA RADDRSNAAK
     HKTRGSHVMV AGVEDDDATK RFAGQLHLSA ADRARRSNVR GKPTGRPGSS SSRRGNDSGR
     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 LGTGVDTLLD 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