ID A0A0L6I1B6_9MICO Unreviewed; 923 AA.
AC A0A0L6I1B6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=AKH00_03230 {ECO:0000313|EMBL:KNY07313.1};
OS Microbacterium sp. GCS4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1692239 {ECO:0000313|EMBL:KNY07313.1, ECO:0000313|Proteomes:UP000037096};
RN [1] {ECO:0000313|Proteomes:UP000037096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GCS4 {ECO:0000313|Proteomes:UP000037096};
RA Jones K.J., Moore K., Sambles C., Love J., Studholme D.J., Aves S.J.;
RT "Genome sequencing of alga-associated bacteria.";
RL Submitted (JUL-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:KNY07313.1}.
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DR EMBL; LGYE01000001; KNY07313.1; -; Genomic_DNA.
DR RefSeq; WP_050721250.1; NZ_LGYE01000001.1.
DR AlphaFoldDB; A0A0L6I1B6; -.
DR STRING; 1692239.AKH00_03230; -.
DR PATRIC; fig|1692239.3.peg.646; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000037096; 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; 1.
DR PRINTS; PR00315; ELONGATNFCT.
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 416..590
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 55..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..215
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 425..432
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 475..479
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 529..532
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 923 AA; 96182 MW; D4F1F5EC62ECE0C5 CRC64;
MAGKPRVHEI AAEFGVDSKV ALAKLKELGE FVKSPSSTIE PPVARKLRAA IEADPSLKSS
GEAAPAAKPA AAKPAAAKSA APTPGPKPGP KPAPAPEAPA APAEAPAATP GPAAAKPGPA
APKSSDGAPK PGAEGGSKPA GDSAPKPGAP RPGNNPFASN QGMGQRPTGP RPGNNPFASA
QGMGQRPTPG NIPRPQAPRP GAPRPGAPRP GSPRPGAPRG GQGGRPGAPF QQRPGGPGRP
GGAGGPGAGG PGARPGGGFA GRPGGGGRGR GPGGGTAGAF GKGGGKSKQR KSRRAKRQEF
EMRSAPVVGG VNVTRGNGET IRMRRGASIA DFADKIETLT GYTVQPGTLV TILFNLGEMA
TATESLDEAT FEVLGEELGY KIQMVSPEDE DKELLEGFGL DLEAELEAES EDDLEIRPPV
VTVMGHVDHG KTRLLDAIRQ TNVIEGEAGG ITQHIGAYQV WTEHEGVERA VTFIDTPGHE
AFTAMRARGA QVTDLAILVV AADDGIMPQT VEALNHAQAA NVPIVVAVNK VDKPEANPAK
VRQQLTEYGL VAEEYGGDVM FVDVSARAGT GIQDLLDAVL LTADAGLDLT ANPNKAARGV
AIEAKLDKGR GSVATVLIQS GTLRVGDAIV AGTAYGRVRA MADENGEQVL EAFPSRPVQV
QGLNSVPRAG DVFIVTEEDR MARQIAEKRE AVERNAQLAK ARKRISLEDF TRALEEGKVE
SLNLIIKGDV SGAVEALEES LLKIEVDESV QLRIIHRGVG AITESDVNLA TIDNAIIVGF
NVRPDTKARE RAQREGVDIR FYSVIYNAID EIESSLKGML KPEYEEVQSG VAEIREVFRS
SKFGNIAGVI VRSGTITRNA KARVIRDGVV LADGLAIESL RRFKDDVTEV RTDYEAGIGL
GKYNDIQIGD EIETTEMVEK PRG
//
