IF2_CHLP8
ID IF2_CHLP8 Reviewed; 939 AA.
AC B3QQI2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Cpar_1793;
OS Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS subsp. thiosulfatophilum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=517417;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 263 / NCIMB 8327;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL Submitted (JUN-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; CP001099; ACF12185.1; -; Genomic_DNA.
DR RefSeq; WP_012503018.1; NC_011027.1.
DR AlphaFoldDB; B3QQI2; -.
DR SMR; B3QQI2; -.
DR STRING; 517417.Cpar_1793; -.
DR EnsemblBacteria; ACF12185; ACF12185; Cpar_1793.
DR KEGG; cpc:Cpar_1793; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3170; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 79988at2; -.
DR Proteomes; UP000008811; 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; 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.
FT CHAIN 1..939
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093768"
FT DOMAIN 436..606
FT /note="tr-type G"
FT REGION 81..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..452
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 470..474
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 492..495
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 546..549
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 582..584
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 153..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 445..452
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 492..496
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 546..549
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 939 AA; 103258 MW; 51E3904119A1C7BA CRC64;
MAIEEKQSRF RISDIARELQ VSPREVLQFV KQEGGKVAST SSMVGEEMRD MIFGNFSQEK
KLVDETRKIR AEKKKRLTRL EEQSRKAYEK EQQLKESLSS APSPAPAAHT PEPVKEPFVE
IPARHEPAVS PAAPAEQPVI AETPQPESPK EEVVATKAPE AEAKPVEQPE KAAETAVEAQ
PEAQSQQEPG AEESAEASQT LVQTLPDSMK TYEAPQKIGG LTVLGTIDVS SGSDRKKKSR
KKSFKENAAE LKDEFEGATS GSSEGGEAGR KKVAKAAGEG ESTTGGEDAS GKKKKGKKKK
KVEVDDKVIS KNIKSTISGM DDSGSSGSRQ KFRKMRRMER ERELEEAEAM REAEKSLIKV
TEYASPHELA ELMGLTAKDI IQKCFTLGKF VTINQRLDKE TIELIAMEFG FDIEFTTEVE
ATTTEEQVDN PEDMKTRPPV VTIMGHVDHG KTSLLDYIRR SNVVAGESGG ITQHIGAYEV
TVEGDRQITF LDTPGHEAFT AMRARGAQVT DIVILVVAAD DSVMPQTIEA INHSKAAGVP
IVVALNKIDK PEANVDKIKT QLSEAGVLVE DWGGEYQCQE ISAKKGIGIS ELMEKVLTEA
EVRELKGNYS RDIMASGIIV ESELDKGKGV VSTVLVQRGF LKVGDPFVAG NSMGKVRALM
DERGKRTDEA GPSTPVRVLG FEDMPQSGDV LTVMESDRDA RDLAQKRQII KREHEFRRST
RVKLDSIARQ IKEGLKKELS VIIKADTDGS IQALADGLMK IHNEEVKVQL IHQGVGQITE
TDVLLAAASD AIIIGFRVRP NVNAKRLAEK EDLDVRFYSV IYHVLEDVEK ALEGMLSPEL
HEESLGSIEI RQVFRVPKVG NVGGAYVLDG KVPRDANVRL LRDGVQIYEG QLDSLKRFKD
DVKEVDSGYE CGLSLKGYDD IKVGDVVEAY KIVEKKRKL
