IF2_PROA2
ID IF2_PROA2 Reviewed; 936 AA.
AC B4S4S6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, 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=Paes_0367;
OS Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=290512;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 271 / SK 413;
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., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
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; CP001108; ACF45424.1; -; Genomic_DNA.
DR RefSeq; WP_012504961.1; NC_011059.1.
DR AlphaFoldDB; B4S4S6; -.
DR SMR; B4S4S6; -.
DR STRING; 290512.Paes_0367; -.
DR EnsemblBacteria; ACF45424; ACF45424; Paes_0367.
DR KEGG; paa:Paes_0367; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 79988at2; -.
DR Proteomes; UP000002725; 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; Reference proteome.
FT CHAIN 1..936
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093812"
FT DOMAIN 433..603
FT /note="tr-type G"
FT REGION 102..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..449
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 467..471
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 489..492
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 543..546
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 579..581
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 107..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 442..449
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 489..493
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 543..546
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 936 AA; 104103 MW; 9932B647728599E0 CRC64;
MSLEEKEMKY RISDIARELQ VSPQEVLHFV KQEGAKVAST SSMVKSDMRE LILGHFSDEK
RLVDQTRKIR EEKRQRLTRL EEQSRKTYEK EQQLKDSIAV FPEPGPVLKK DHVHEEPEKP
AIVISESEPE VEPEVEPEQP AAAQEAEEAV PTEAVSVPEP VEQERVVPAP EKPEAEKPVP
EQSSTMKAQA SPEMQVTYEK PKNIGGLTVL GSIDVRSALD RGSESDRKKK NRKKRFKEQA
DELKGEFENA GKAEGDKKPA KSGEAKTKAP KKAAGTTGSA AEDTTSSKKK KGGKKKKPAV
DEKVISQNIR STISGMDDSS GGSGSRQKFR KMRKIEREKE LEAAEAVKEA ERSIVRVTEF
ATAHELADLM GITAKEIIQR CFTLGKFVTI NQRLDKETIE LVALEFGFEA EFVSEVEATE
VFEVHDDSED LEIRPPVVTI MGHVDHGKTS LLDYIRSSNV VAGESGGITQ HIGAYEVTLD
NGRSITFLDT PGHEAFTAMR ARGAQVTDIV ILVVAADDSV MPQTIEAINH SKAANVPIVV
AINKIDKPEA NPEKIRAQLS EAGVLVEDWG GEYQCQEISA KQGMGMHELM EKVLMEAEIR
ELKANFSREA NSRGIIVESE LDKGKGVIST VLVQRGFLKV GDPFVAGNTM GRVRALMDER
GRRIKEAGPS QPVRVLGFED LPQSGDEFVV MPTDKEAREI AQKRQIIRRE HEFRRSTRVK
LDSIARQIKE GLMKELSVII KADTDGSIQA LADGLMKIHN EEVKVQIIHQ GVGQITETDV
LLAAASDAII IGFRVRPNVN AKRLAEKEDL DVRFYSVIYH VIEEIEQALE GMLSPELHEE
SLGSLEIRQV FRVPKIGNVG GCYMLEGKIF RDSKVRLLRE GVQIYDGVLD SLKRFKDDVK
EVDAGYECGL NLKGYGDIKV GDIVEAYRIV EKKRKL
