IF2_CHLPM
ID IF2_CHLPM Reviewed; 900 AA.
AC A4SGG2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, 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}; OrderedLocusNames=Cvib_1561;
OS Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris
OS vibrioformis (strain DSM 265)).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 265 / 1930;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J.,
RA Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J.,
RA Schuster S.C., Bryant D.A., Richardson P.;
RT "Complete sequence of Prosthecochloris vibrioformis DSM 265.";
RL Submitted (MAR-2007) 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; CP000607; ABP37571.1; -; Genomic_DNA.
DR RefSeq; WP_011890794.1; NC_009337.1.
DR AlphaFoldDB; A4SGG2; -.
DR SMR; A4SGG2; -.
DR STRING; 290318.Cvib_1561; -.
DR EnsemblBacteria; ABP37571; ABP37571; Cvib_1561.
DR KEGG; pvi:Cvib_1561; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 79988at2; -.
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.
FT CHAIN 1..900
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075613"
FT DOMAIN 397..567
FT /note="tr-type G"
FT REGION 80..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..413
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 431..435
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 453..456
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 507..510
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 543..545
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 80..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 406..413
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 453..457
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 507..510
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 900 AA; 98879 MW; B7BA10593A561398 CRC64;
MALEDMDKKY RISDIARELQ VSPQEVLRFV KQEGARVAST SSMVDTEMHG LILGQFSDEK
KMVDETRKIR AEKKQRLNRL EEQSRKTVEK EDQLRDTLQP SPVPGRVEVP VPAPIEAPVA
APVVPDAPVA PVEVVPPAPP EAPLMAEAAV EAEPEVAPPS LEAEEDSPVE AQANDQIVSY
DAPKNIGGLT VLGTLDMESE SDRKRRGKKK NFKESADALK DEFDTTGSVE LDDDGKPKKK
PGSSPLGSDL GMGKKKGKKK KKPEVDEKVI SANIRSTISG MDVGAGSGSR SKFRKQRKME
REHEQEEADA FREMQQQVVR VTEYASPHEL AELMSVTAKD IIQKCFTLGK FVTINQRLDK
ESIELIALEF GYEAEFVSEV EATEVVAEVD NEEDMDTRPP VVTIMGHVDH GKTSLLDYMR
NSNVAGGESG GITQHVAAYE VTGSNGRKIT FLDTPGHEAF TAMRARGAQV TDIVILVVAA
DDSVMPQTIE AINHAKAAGV PIVVAINKID KPEANPEKIK TQLSEAGVLV EEWGGENQCQ
EISAKKGTGI VELMEKVLTE AEVRELKGNY SKEVLASGVI VESELDKGKG VISTVLVQRG
FLKVGDPFVA GNTMGKVRAI MDERGKRIQS AGPSRPVSVL GFEDLPQSGD VLTVMASDRE
ARDLAQKRQV IRREHEFRRS TRVKLDSISR QIKEGLMKEL SVIIKADTDG SIQALADGLM
KIQNDEVKVQ IIHQGVGQIT ETDVLLAAAS DAIIIGFRVR PNVNAKRLAE KEDLDVRFYS
VIYHVLEDVE KALEGMLSPE LHEESLGSLE IRQVFKVPKV GNVGGCYVLD GKILRDAKVR
LLRDGVQIYD GTLDTLRRFK DDVKEVDAGY ECGVGLKNYD DIKVGDVVEA YRIVETKRKL
