ID A0A0S7YLP6_9BACT Unreviewed; 944 AA.
AC A0A0S7YLP6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 ORFNames=AMS14_03465 {ECO:0000313|EMBL:KPJ75510.1};
OS Planctomycetes bacterium DG_20.
OC Bacteria; Planctomycetota.
OX NCBI_TaxID=1703413 {ECO:0000313|EMBL:KPJ75510.1, ECO:0000313|Proteomes:UP000052133};
RN [1] {ECO:0000313|EMBL:KPJ75510.1, ECO:0000313|Proteomes:UP000052133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_20 {ECO:0000313|EMBL:KPJ75510.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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 -!- 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPJ75510.1}.
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DR EMBL; LIZP01000057; KPJ75510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7YLP6; -.
DR PATRIC; fig|1703413.3.peg.208; -.
DR Proteomes; UP000052133; Unassembled WGS sequence.
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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 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; 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; PF04760; IF2_N; 2.
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.
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}.
FT DOMAIN 443..612
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 37..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..594
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 97..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 452..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 498..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 552..555
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 944 AA; 102668 MW; 5206D08F5E3AAD02 CRC64;
MPSKEVLEIC REVGLEVKSH SSTIDEDEAD QVRRRLAAFL GDEPEEEEPG PGPTAGTLAA
RLVEPPPKPA EPELSPEEQL EQARKRVIAL PSRGFKKPKA EGLKLPSRRK PPARRPPAEA
PAVEAEAPAA VEEMPAAEEM PVAEAAEPAA VEEQPVAEAP AEAAAPMAEA PGIEAPAPPA
ERRERRRLPR RPPGPKLAPK PKLAPRPKLA PKPLRHPQKV AEPAAPPEPH PQAIGVGAPK
KRKPPGRPSK PRARPAAAVV DEAVAAPPKE AAPAARRGRR RGKRAPEPET EGMRKAQAFR
RRERIRKREE MDDVAALDGI GAGGPILSSE RARLGRTGRP VAARPSRGVP RPHVPEGPKK
AVVEMPMTVK DLSAALGIRA GDIIKHLMVQ GVMAAINDTL TDEQVLDVAL SRDIEIEVRH
ERRPADVIRE MEQREDLPEA LQPRPPIVTF LGHVDHGKTS LMDFIRKSRV VDGEAGGITQ
HIGAYRVHVG ERWITFLDTP GHEAFTAMRA RGARVTDVAV LVIAADDGIM PQTEEAINHA
KAAGVPIVVA INKCDLPQAN SDRVKQQLTQ YELLTEEWGG QTICIETSAI TGQNVDRLLE
SLLLEAEMIE LKANPDRAAV GTVIEAELAG GFGPMATLLV QKGTLEAGNV VLAGTAWGKI
RAMTDENRKR LRRAGPTVPV RVAGLSGVPE AGDRFYVLDD LSLAKQLAED REWSQREAEL
AEQRRPRTLE AVFEQMTAEE AKELPVIIKA DVQGSVEAIR ENLEKIEHPE VRVRVIHAAV
GGVNESDVLL ADASDAIIIG FNAVPDHAAR LLAEERGVDI RPYNIIYNVT DDVRKALEGL
LAPLEEERHL GECEVLQTFK ISRVGTIAGC RMTDGVINRN ARLRVIRDGL VVYAGRIESL
KRFKDDVREA RAGQECGIHI AGYNDIKVGD RIEAYETVSV ARTL
//
