ID   IF2_HERAR               Reviewed;         941 AA.
AC   A4G7S7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=HEAR2433;
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1;
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.-C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU207211; CAL62564.1; -; Genomic_DNA.
DR   RefSeq; WP_011871826.1; NC_009138.1.
DR   AlphaFoldDB; A4G7S7; -.
DR   SMR; A4G7S7; -.
DR   STRING; 204773.HEAR2433; -.
DR   PRIDE; A4G7S7; -.
DR   EnsemblBacteria; CAL62564; CAL62564; HEAR2433.
DR   KEGG; har:HEAR2433; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_0_4; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000006697; 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; 2.
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; Reference proteome.
FT   CHAIN           1..941
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008254"
FT   DOMAIN          441..610
FT                   /note="tr-type G"
FT   REGION          170..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..457
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          475..479
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          496..499
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          550..553
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          586..588
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        271..294
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..350
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         450..457
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         496..500
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         550..553
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   941 AA;  101593 MW;  11B0F23DFA099E7D CRC64;
     MASNNVAQFA TELKMPADVL LTQLRDAGVE KSSTSDELSK ADKDKLLEHL RRAHGVAPDG
     EKKKITLMRK ETTEIKQADA TGKSRTIQVE VRKKRTFVKR DEPAAEEAPV VVAAPIIDAA
     EVERRAEESR RHAELMARQE ADLREKQERL AKLEAEKETQ AKALKKAEVD AQKAEVDAQK
     AEAEKPVEVK ADESAIEEKK RVAAEESKKK AAAAAKEAAK EANEKAAATE LARKVVADEV
     AQIKAMMNAP RRAIKAPEPV APVAKPAAEG TLHKPADKKP GEKKDEKKPA VTADKKSIKS
     ANVSSTWQDD AKKRSAGIKT RGNTGGGRDG WRAGTKGRRQ SHHDDRESNF QAPTEAVVKD
     VQVPETITVA ELAHKMSVKA SEVIKQLMKL GQMCTINQVL DQETAMILVE EMGHVAHAAK
     LDDPEALLEI GAEQADVEAL PRAPVVTVMG HVDHGKTSLL DYIRRAKVAT GEAGGITQHI
     GAYHVETPRG MITFLDTPGH EAFTAMRARG AKATDIVILV VAADDGVMPQ TKEAIAHAKA
     AGVPLVVAIN KIDKPSANLD RVKQELIAEQ VVPEEYGGDS PFVPVSAKTG EGIDALLEQV
     LLQAEVLELK APVVSPARGL VVEAKLDKGR GPVATILVQS GTLRRGDVVL AGSAYGRVRA
     MLDENGKSIS EAGPSIPVEI QGLTEVPNAG EEVMVMADER KAREIGLFRQ GKFRDVKLAK
     QQAAKLENMF ENMGEGEVKN LPMIIKTDVQ GSQEALVGSL QKLSTGEVRV QVVHAAVGGI
     SESDVNLAVA SKAVIIGFNT RADASARKLA EANGVDIRYY NIIYDAVDEI KAAMSGMLSP
     EKREQALGLV EIRQVILVSK VGAIAGCYVL EGVVKRGASV RLLRDNVVIW TGELDSLKRF
     KDDAKEVKFG FECGLTLKNF NDIKEGDQLE VFEVQEIART L