ID A0A0Q8PQU0_9ACTN Unreviewed; 958 AA.
AC A0A0Q8PQU0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=ASE01_13525 {ECO:0000313|EMBL:KRB76051.1};
OS Nocardioides sp. Root190.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB76051.1, ECO:0000313|Proteomes:UP000050886};
RN [1] {ECO:0000313|EMBL:KRB76051.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB76051.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB76051.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB76051.1,
RC ECO:0000313|Proteomes:UP000050886};
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:KRB76051.1}.
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DR EMBL; LMIA01000010; KRB76051.1; -; Genomic_DNA.
DR RefSeq; WP_056753328.1; NZ_LMIA01000010.1.
DR AlphaFoldDB; A0A0Q8PQU0; -.
DR STRING; 1736488.ASE01_13525; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000050886; 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; 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; PF04760; IF2_N; 2.
DR PRINTS; PR01217; PRICHEXTENSN.
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}; Reference proteome {ECO:0000313|Proteomes:UP000050886}.
FT DOMAIN 451..623
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 60..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 460..467
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 510..514
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 564..567
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 958 AA; 98988 MW; A70B6FCDB697F181 CRC64;
MAKTRVSELA KKYGIPSKEA LEKLSAIGEF AKTASSSVEL PAVKKFESTY GAELLAKMQP
SGDAGAAAPA KPAPRPAPRK PAEAPAPVEA PAAAEAPAPV EAAAPAPVAP VEDKPAAPRP
GPRPGPAKAP EPEPEPTPEP PAPVAEAPAP AAAKPAGPKP PTPKAPAPAP RPVGKPGGTP
RPGNNPFAPS QGMGRRPAPA PREGDAGPAG PRPPAGAGGA AARPGMPRPN PAMMPKSPAA
FGQGPGGRGP GGPGAGRGPG GPGGRPGGPG RPGAPGRGGP GGAGAGAGAG APGRGPGGFG
PGGGGRPGGG RPGQRGQTQG AFGRPGGPAR RGRKSKRARR QEFEAMEAPT IGGMRVRKGS
GETIRLARGC SLTDFADKIG VDAASLVQML FHLGEMVTAT QSVGDETLEL IGDELNYVVE
IVSPEDEDRE LLETFDLEFG ADEGGEDDLV IRPPVVTVMG HVDHGKTKLL DALRDANVVA
GEAGGITQHI GAYQVHTEVD GNDRRITFID TPGHEAFTSM RARGAQATDI AVLVVAADDG
VMPQTVEALN HARAAGVPIV VAVNKIDKES ADPTKVRGQL SEYGLVPEEY GGDSMFVDVS
AKAGLNLDKL LEAIVLTADA SLDLRANPVQ DAQGLVIEAH LDRGRGPVAT ILVQRGTLRV
GDSIVAGPAH GRVRAMLDEH GDNIVEADPS RPAMVLGLTA VPGAGQNFLV VEDDRMARQI
AEKREARERA AMQAKRRVRR TLEDFMASME KGESQELNLI LKGDVSGSVE ALEDALAQID
VGEEVSLRVI DRGVGAITET NVDLAAASDA IIIGFNVRPQ GKAGQMADKE GVEIRYYSVI
YQAIEEIEAA LKGMLKPEYE ESTLGQAEIR AIFRSSKIGN IAGCMVIGGV LRRNAKVRIL
RDGAVVADNL DLASLKREKD DASEVREGFE CGLVLKNFQD IKEGDIVEAF EMKEIPRS
//
