ID   IF2_DESAL               Reviewed;        1040 AA.
AC   B8FCY5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 88.
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=Dalk_4738;
OS   Desulfatibacillum aliphaticivorans.
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfatibacillaceae; Desulfatibacillum.
OX   NCBI_TaxID=218208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK-01;
RX   PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA   Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA   Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT   "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT   for anaerobic alkane oxidation.";
RL   Environ. Microbiol. 14:101-113(2012).
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; CP001322; ACL06416.1; -; Genomic_DNA.
DR   RefSeq; WP_015949455.1; NC_011768.1.
DR   AlphaFoldDB; B8FCY5; -.
DR   SMR; B8FCY5; -.
DR   KEGG; dal:Dalk_4738; -.
DR   eggNOG; COG0532; Bacteria.
DR   eggNOG; COG3064; Bacteria.
DR   HOGENOM; CLU_006301_5_1_7; -.
DR   Proteomes; UP000000739; 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; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 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; IPR004161; EFTu-like_2.
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; PF04760; IF2_N; 2.
DR   PRINTS; PR00449; RASTRNSFRMNG.
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..1040
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000190631"
FT   DOMAIN          539..706
FT                   /note="tr-type G"
FT   REGION          73..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..555
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          573..577
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          594..597
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          648..651
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          684..686
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        74..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..375
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         548..555
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         594..598
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         648..651
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1040 AA;  111922 MW;  B612112D07102DB3 CRC64;
     MAKLRVHELA RELNMTNKVL LDKLQAMDLP TPVRSHMSSL DDDVVALVKA SLVRPKAKSV
     VEKRIGTTVI RRRKKVVKPA EGGPEETAKP EEGAEEGVQE MDAAQESVSA PEAEKAPEPV
     AEKAPEPQKA APAAEEPKAE EGAPAPEKAA PVQAKEEPEE APQAEAKPAP PKKVDVTPPG
     DKAKIIAKPE PPQPAEPEPP KEEPAPVELP EEKQAVSAKA ADTPAEPQEE PEAKPEIKAE
     AKAEEGAPEK PAEEPKAKEE QKAAPEDSKE EPKAEEPAQP AEDEKAEEKA KAPEEKEPAK
     SQEPQAAKEP SKEAPKPKGK KKKKKETAAK IISLPTRPVE PVVPPASRQK PAPQSPAGPG
     GPGGPGVPPQ PRAPQDLGGD PAAKKEKRKK KGRRDGGTTE ETDSKFFKKK ISFRKKAVVE
     GADLYDKTPG KLRKGKKGGK AQPVRQQKTQ TTTPKAIKRR IKIDEAIAVA DLAKRLGIKA
     AELIKNLMGM GIMATVNQML DYDTAVLLAA EFGYEVEKAN FEEETVLKAE EDAPETLSNR
     PPVVTIMGHV DHGKTSLLDA IRESNVTGGE AGGITQHIGA YLVDSPRGRI AFLDTPGHEA
     FTAMRARGAQ VTDIVILVVA ADDGVMPQTV EAVNHSKAAG VPIIVAVNKM DKEGADPDRV
     MRELSDHGLV PEDWGGDTIF VQVSAKQRQG LDDLLEMVLL QAEVLELQAN PDKLARGHVV
     EAKVDPGRGP VATVLIQEGT LHAGDVVVCG IHYGKVRAMY NEKRQPLDAA GPACPAEILG
     LSGVPMAGDE IIAVDDEKVA KQVSSHRAQK QRATELAKSS KLSLDNLFDQ MQAGNVKDLN
     LIIKADVQGS IEALRESLEK LSGDEVKIHV VHAATGTVLE SDVALAAVSN AIIVAFNVRP
     SPKVSDMAAE EHVDIRFYDI IYNAINEIKD AIVGLMESTY KEHVSGRAEV RDTFTIPKVG
     TIAGCYVTDG KVERHNQVRL LRDGVVIFDG KLSSLRRFKD DVKEVATGYE CGMGIENFND
     IKIGDVLELY YLEEIKPVLK
//