ID   IF2_SULDN               Reviewed;         874 AA.
AC   Q30SS6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   02-SEP-2026, entry version 123.
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=Suden_0676;
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS   denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC   Campylobacterales; Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=326298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33889 / DSM 1251;
RX   PubMed=18065616; DOI=10.1128/aem.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA   Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA   Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA   Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA   Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA   Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(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; CP000153; ABB43955.1; -; Genomic_DNA.
DR   RefSeq; WP_011372309.1; NC_007575.1.
DR   AlphaFoldDB; Q30SS6; -.
DR   SMR; Q30SS6; -.
DR   STRING; 326298.Suden_0676; -.
DR   KEGG; tdn:Suden_0676; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_4_1_7; -.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000002714; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
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   FunFam; 2.40.30.10:FF:000008; Translation initiation factor IF-2; 1.
DR   FunFam; 2.40.30.10:FF:000054; Translation initiation factor IF-2; 1.
DR   FunFam; 3.40.50.10050:FF:000001; Translation initiation factor IF-2; 1.
DR   FunFam; 3.40.50.300:FF:000019; Translation initiation factor IF-2; 1.
DR   Gene3D; 1.10.10.2480; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR053905; EF-G-like_DII.
DR   InterPro; IPR044145; IF2_II.
DR   InterPro; IPR006847; IF2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
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; PF22042; EF-G_D2; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Reference proteome.
FT   CHAIN           1..874
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000335513"
FT   DOMAIN          374..543
FT                   /note="tr-type G"
FT   REGION          55..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..390
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          408..412
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          429..432
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          483..486
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          519..521
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        56..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         383..390
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         429..433
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         483..486
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   874 AA;  95935 MW;  6B19F540A06F3905 CRC64;
     MTEKVRVHEI AKELGITSKD VVKKASDMGI EIKSANSSVS MEEAEGLMNY IMSGELAQSP
     TAEQKVQTKA PSHTPKEEDP TQESNKSQTT LSKKASETPI QHVVEKAKEI DVKNSEKEVI
     SEVKEIKKEE ESIESSELKK MQIKKSGLKI VKKKQPREEE KIQDDFISSV KQTQASISSY
     GKISAEVLEE LANKKKAKQA SSGAKKQEQG VKIDIFGASL SEVSMDMDDQ IVLLDLNSTQ
     RQELIAEEPR KPKVVKPAGR NANKKSAPKG RNVSRDKRKK YAKDKPEDLI VTHVEIPEDI
     RVYEFAEKLN RPISDVIKVL FSLGLMMTKN DFLGSDEIEI LSEEFGVEVT IVDPKDAFNY
     EEDLAEVIDE NATERPPVIT IMGHVDHGKT SLLDAIRKAK VTQDEAGGIT QHIGAYTIEQ
     NGKAITFLDT PGHAAFSQMR QRGTDVTDII IIVVAADDGV KPQTEEVIKL AKESKVPVIV
     AVNKMDKPTA NPDMVKAQMA ERGLNPIDWG GDIEFIPISA KSGMGIDELL ENILLTAEVL
     ELKANENAMA KAAVVESSLE KGRGPVATVI VQNGTLNVGD YVVCGSSYGR VKALINEHKQ
     QIKSIKPSHT AVVVGLNEVP SSGEIMMAMS SDKEAREYAL KRHEYDRHKE LSHSTKSTLE
     DMTSMIAEGR LKSLKVVLKT DVHGSLEAIR SSLNELRNDE VKINVISSGV GGITENDVEL
     VSNSENCVLL GFNVRPTGSV KALAKQKNVD IKTYSIIYQL LDDMTGMLMG MMAPKFSEIN
     TGQAEVRNTF KAPKGMVAGC VVVDGKLIRG GLVRVIRDGV VVHEGELTSL KRFKDDVDEI
     GNGYECGVMI KGYDDVIVGD VIETFKKVEQ KVSL
//