IF2_LEPCP
ID IF2_LEPCP Reviewed; 991 AA.
AC B1XY67;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Lcho_1701;
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Leptothrix.
OX NCBI_TaxID=395495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001013; ACB33968.1; -; Genomic_DNA.
DR RefSeq; WP_012346729.1; NC_010524.1.
DR AlphaFoldDB; B1XY67; -.
DR SMR; B1XY67; -.
DR STRING; 395495.Lcho_1701; -.
DR PRIDE; B1XY67; -.
DR EnsemblBacteria; ACB33968; ACB33968; Lcho_1701.
DR KEGG; lch:Lcho_1701; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; RDVMMAG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001693; 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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..991
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093800"
FT DOMAIN 491..658
FT /note="tr-type G"
FT REGION 53..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..507
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 525..529
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 546..549
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 600..603
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 636..638
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 115..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 500..507
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 546..550
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 600..603
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 991 AA; 104938 MW; E523EE5B26F2CF47 CRC64;
MAVTTVAQFA TELNRPASTL LEQLQHAGVS KASASDPLTD TDKEKLLAYL RTSHGTSGAD
RKKITLTKKS TSEIKQADAS GKARTIQVEV RKKRVFVKRD DPTGASSESH DSQDVQELSA
AEEAELQRRE EEALREAEAL RRQQEEEAAQ RQRAAEEQAR QEREARERAE REAAERAAAE
AAARVAAEAA AALAAAEKAA ATAPAPAPVA AVVPKAPAPA PVVAAPTLAV ASLGAKPVAP
APTSGMRVIK AADIVAGEAQ KQIDLDKRRK AAEAEAAAIR AMMAAPKKVM VAKKPEEPKP
VVPAAGAVGK DGIKGTIHRP KTAAGAPAPG AAPGAAAKPG EKKSVKSEKL SSSWADDAKK
RGAAAPASKG RAPDVRGGWK APGGARGGRR GDRGGAVSNF TPPADVQIHE VHVPETISVA
DLAHKMSVKG SEVIKQLMRL GQMVTINQQL DQETAMIVVE EMGHKAFAAK LDDPDAFLEE
ENLAEAGESL PRPPVVTVMG HVDHGKTSLL DYIRTSRVAA GEAGGITQHI GAYHVETPRG
VITFLDTPGH EAFTAMRARG AKATDIVILV VAADDGVMPQ TKEAIAHSKA AGVPIVVAIN
KIDKPDSNLD RVRSELVAEG VVPEEFGGDA PFCLVSAKTG QGIDTLLEQV LLQAEVLELN
APQEALAKGL VIEARLDKGR GPVATVLVQS GTLKRGDVVL AGQSYGRVRA MLDETGKAAQ
EAGPSIPVEI QGLTEVPSAG DEFMVLADER RAREIATFRQ GKYREVNLNR RQAAKLENMF
ENMGQGAAQT LALIIKADVQ GSQEALAASL LKLSTDEVKV QIVHAAVGGI SESDVNLALA
SKAVIIGFNV RADAGARKLA DGNDVDLRYY NVIYDAVDEI KSAMSGMLAP EQREEAIGTA
EIRTVFVATK IGTIAGSMVT SGLVRRNCRF RLLRNNIVIY TGEVDSVRRL KDDVKEVKEG
FECGIKLKNY TDIAEGDQLE FFEIKEVART L
