IF2_CHLL3
ID IF2_CHLL3 Reviewed; 915 AA.
AC Q3B1Z8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Plut_1779;
OS Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon
OS luteolum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=319225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 273 / BCRC 81028 / 2530;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelodictyon luteolum DSM 273.";
RL Submitted (AUG-2005) 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; CP000096; ABB24633.1; -; Genomic_DNA.
DR RefSeq; WP_011358505.1; NC_007512.1.
DR AlphaFoldDB; Q3B1Z8; -.
DR SMR; Q3B1Z8; -.
DR STRING; 319225.Plut_1779; -.
DR PRIDE; Q3B1Z8; -.
DR EnsemblBacteria; ABB24633; ABB24633; Plut_1779.
DR KEGG; plt:Plut_1779; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 79988at2; -.
DR Proteomes; UP000002709; 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.
FT CHAIN 1..915
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228224"
FT DOMAIN 412..582
FT /note="tr-type G"
FT REGION 83..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..428
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 446..450
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 468..471
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 522..525
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 558..560
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 102..116
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 421..428
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 468..472
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 522..525
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 915 AA; 99922 MW; 89FD9101A9E86A7D CRC64;
MAVEDMDKKY RISDIARELQ VSPQEVLRFV KEGGAKVAST SSMVDSEMRG LIFAEFSNEK
KMVDETRKIR AEKQLRLTRL EEQSRRAVEK EQILRETLTP SPAPPVHEPP VRAAAQPAPV
PVAAGEAPSP LAPETPAPAT ESAPAVAPAG VPAAEPVSEA LSAPLPEPVP EPVPEPPAPE
VVAVVEAVPN DQIVSYDAPK NIGGLTVLGT LDMQSEADRK KKGKKKNFRE QAVALKDEFE
TPSSTTLDED GVPKKKPVAG VQPEGFGVGK KKGKKKKPAV DDKVISANIR TTISGMDDSS
GTGSRSKFRK QRKMEREREQ EEADLLRESE QQIMRVTEYA SPHELAELMG VTAKDIIQKC
FALGKFVTIN QRLDKESIEL IALEFGFEAE FISEVEATAV EAVVDRDEDL ETRPPVVTIM
GHVDHGKTSL LDYIRNSNVV AGESGGITQH VAAYEVTASN GRKITFLDTP GHEAFTAMRA
RGAQVTDIVI LVVAADDSVM PQTIEAINHA KAAGVPIVVA INKMDKPEAN PEKIKTQLSE
AGVLVEEWGG ESQCQEISAK KGLGIEELME KVLTEAEMRE LKGNFSKDVP ATGVIVESEL
DKGKGVISAV LVQRGYLKVG DPFVAGNIMG KVRALMDERG KRIPSAGPSQ PVSVLGFEDL
PQAGDVLTVM ASDKEARDLA QKRQIIRREH EFRRSTRVKL DSIARQIKEG LMKELSVIIK
ADTDGSIQAL ADGLMKIQNE EVKVQIIHQG VGQITETDVL LAAASDAIII GFRVRPNVNA
KKLAEKEDLD VRFYSVIYHV LEDVEKALEG MLSPELHEES LGSLEIRQVF RVPKVGNVGG
CHVLEGKILR DAKVRLLRDG VQIYDGMLDT LRRFKDDVKE VDAGYECGVG LKNYDDIKVG
DVVEAYRIVE KKRKL
