ID A0A0H5BFN3_BLAVI Unreviewed; 931 AA.
AC A0A0H5BFN3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100,
GN ECO:0000313|EMBL:CUU43511.1};
GN ORFNames=BV133_1583 {ECO:0000313|EMBL:BAR99176.1}, BVIRIDIS_25330
GN {ECO:0000313|EMBL:CUU43511.1};
OS Blastochloris viridis (Rhodopseudomonas viridis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Blastochloridaceae; Blastochloris.
OX NCBI_TaxID=1079 {ECO:0000313|EMBL:CUU43511.1, ECO:0000313|Proteomes:UP000065734};
RN [1] {ECO:0000313|EMBL:BAR99176.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 133 {ECO:0000313|EMBL:BAR99176.1};
RA Tsukatani Y., Hirose Y., Harada J., Misawa N., Mori K., Inoue K.,
RA Tamiaki H.;
RT "Complete Genome Sequence of the Bacteriochlorophyll b-Producing
RT Photosynthetic Bacterium Blastochloris viridis.";
RL Genome Announc. 3:e01006-15(2015).
RN [2] {ECO:0000313|EMBL:CUU43511.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1 {ECO:0000313|EMBL:CUU43511.1};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000065734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19567 / DSM 133 / F {ECO:0000313|Proteomes:UP000065734};
RX PubMed=26798090; DOI=10.1128/genomeA.01520-15;
RA Liu L.N., Faulkner M., Liu X., Huang F., Darby A.C., Hall N.;
RT "Revised genome sequence of the purple photosynthetic bacterium
RT Blastochloris viridis.";
RL Genome Announc. 4:0-0(2016).
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:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000645}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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DR EMBL; AP014854; BAR99176.1; -; Genomic_DNA.
DR EMBL; LN907867; CUU43511.1; -; Genomic_DNA.
DR RefSeq; WP_055038371.1; NZ_LN907867.1.
DR AlphaFoldDB; A0A0H5BFN3; -.
DR STRING; 1079.BVIR_3089; -.
DR KEGG; bvr:BVIR_3089; -.
DR PATRIC; fig|1079.6.peg.3250; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000065734; Chromosome I.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR004161; EFTu-like_2.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000065734}.
FT DOMAIN 428..598
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 437..444
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 484..488
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 538..541
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 931 AA; 99115 MW; 0EF318740EC9ADD5 CRC64;
MTETKSPGDK TLSVSKTLTL KRPSESGVVR QSFSHGRSKA VVVEKVKRRT GPGEAGGQSG
SAPAPAKPAS VTTPLSTKPR VGGPPASPSA GTRPSGVVLR TLTDDERDAR TQALQEARVR
EADERRAAVE EARRRIEREA KERVEREAAE ARKREEEARR ALEDEARRKA EQEARKRFGE
EEAARRAAGA PAQASSASQS PSSRPPYRSG GPGSGPRPAG AGPRPAGAGG PRSSGPGGGA
PRPGGAGAPA MARPGGAAAP GRPGAPGGEE EEARRARRPS GGGPAKPVIP PKAPKATPGE
EKRRGRLTVV TAYQEGEQRE RSVAAFRRRV QRMTGQRQSE TKEKISREVT IPETITIQDL
ANRMSERAVD VIRMLMRQGQ MMKINDVIDA DTAQLIAEEL GHTVKRVAEA DVEEGLFDTP
DDPEALQPRP PVVTIMGHVD HGKTSLLDAI RHTHVVAGEA GGITQHIGAY QVTAPSGGRV
TFIDTPGHAA FTAMRARGAK VTDVVVLVVA ADDGVMPQTI EAINHAKAAK VPLIVAINKI
DKPDAKPERV RTELLQHSIV VESMGGDTLE VEVSAKQKLN LDKLLEAVAL QAEVLDLKSN
PARPAEGTVI EGKLDRGRGP VATVLVQRGT LKVGDIVVAG AEWGRVRALV ADTGVQVDTA
GPSLPVEVLG FNGTPEAGDR LAVVENEARA REVADYRSRQ RRDKAAAKIT GRGSLAEMMK
ELKAGAGRKE FTLLVKADVQ GSLEAIVGSL DKLGTDEVMA RVVHSGVGGI SESDVTLAAA
SGAAIIGFNV RAHKEAREAA ERSGIEIRYY NIIYDLVDDV KQAMSGLLPP TVREIMLGNA
LVLEVFNITK VGKIAGCRVT DGTVERGAHV RLIRDNVVIH EGKLSQLKRF KDDAKEVLAG
QECGMSFENY QDMRAGDVIE CYRVETVKRS L
//
