IF2_DESAL
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 03-AUG-2022, entry version 80.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Dalk_4738;
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfobacteraceae; 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 PRIDE; B8FCY5; -.
DR EnsemblBacteria; ACL06416; ACL06416; Dalk_4738.
DR KEGG; dal:Dalk_4738; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3064; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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; 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; 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; PF04760; IF2_N; 2.
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..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
