ID A0A0Q4KNW3_9SPHN Unreviewed; 948 AA.
AC A0A0Q4KNW3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=ASF00_15190 {ECO:0000313|EMBL:KQN24199.1};
OS Sphingomonas sp. Leaf34.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736216 {ECO:0000313|EMBL:KQN24199.1, ECO:0000313|Proteomes:UP000051932};
RN [1] {ECO:0000313|EMBL:KQN24199.1, ECO:0000313|Proteomes:UP000051932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf34 {ECO:0000313|EMBL:KQN24199.1,
RC ECO:0000313|Proteomes:UP000051932};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN24199.1, ECO:0000313|Proteomes:UP000051932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf34 {ECO:0000313|EMBL:KQN24199.1,
RC ECO:0000313|Proteomes:UP000051932};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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: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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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:KQN24199.1}.
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DR EMBL; LMLC01000005; KQN24199.1; -; Genomic_DNA.
DR RefSeq; WP_055881139.1; NZ_LMLC01000005.1.
DR AlphaFoldDB; A0A0Q4KNW3; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000051932; 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; 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; 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; 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|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 447..617
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..268
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 456..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 503..507
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 557..560
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 948 AA; 100189 MW; F7ED040533852DC5 CRC64;
MSDTDNEKPK LGMRAPLGVK RTVETGQVKQ SFSHGRSNTV IVETKRARVL RRPGEPDVQV
ADAAPIAAPA PAAAPAAPAP QARAPQPAPA PVRQQQSNLS PQERQAKLLR EAEEQRMNTL
EEGRRRQEAE RAKAIEDERN RVAERARAEA EAKAPKPVEA PAPAPAPVVE AAPAPVAAPT
PAPAPAPVEA PVAAAPAPAP VAAPKPAPAP VAAAPAPAPK PAPAPVAPPA PPPIIELTRD
PAFPAPRRFS PVARPERPPP PPKPVAAPAA AAPATTGNAG TTAARPGATG ANAPAGGVRR
DAVPARPQQR DRKGDDRRTS GKLTVNRALG DGDGARARSL AALKRAREKE RRGTGGPREA
QAKQIRDVVV PEAITVQELA NRMAEKGADL VKALFKMGMP VTMTQTIDQD TAELLVTEFG
HNLTRVSDVD QDLANDTIDD AEETLKPRAP VVTIMGHVDH GKTSLLDALR GTDVVRGEAG
GITQHIGAYQ VTLKDKSKIT FLDTPGHEAF TQMRARGADV TDIVILVVAA DDGLMPQTVE
AIAHTKAAGV PMIVAINKID KEGANAQKVR ERLLSEEIVV EDMGGDVQDV EVSATKKIGL
DTLIEKIQLQ AELLELRANP DRAAEGTVIE AKLDKGRGPV ATILVNRGTL KVGDIFVVGG
ESGKVRALVD DKGKQIKEAG PAMPVEVLGL SGVPSAGDPF QVVENEARAR EVAEYRRSVK
TDKRTASVPA SLESMFSALK EKQAIEYPLV VKADTQGTVE AIVGAINKIS TDLIKARVLS
SGVGGITESD VTLAAASGAP IIGFNVRPNA KAREIAERQK VAFKYYDVIY DLIDEIRAGM
AGELGPEAFE TVVGRADIRE VFSAGKHGKA AGLLVTEGNI RKALKARITR NDVIIYQGEI
ASLRRFKDDV AEVRAGLECG VTFTSNFVDI KAGDVLETFE VEMRERTL
//
