ID A0A0Q5LQL4_9MICO Unreviewed; 922 AA.
AC A0A0Q5LQL4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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=ASF88_13345 {ECO:0000313|EMBL:KQR52507.1};
OS Leifsonia sp. Leaf336.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736341 {ECO:0000313|EMBL:KQR52507.1, ECO:0000313|Proteomes:UP000050966};
RN [1] {ECO:0000313|EMBL:KQR52507.1, ECO:0000313|Proteomes:UP000050966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf336 {ECO:0000313|EMBL:KQR52507.1,
RC ECO:0000313|Proteomes:UP000050966};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR52507.1, ECO:0000313|Proteomes:UP000050966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf336 {ECO:0000313|EMBL:KQR52507.1,
RC ECO:0000313|Proteomes:UP000050966};
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:KQR52507.1}.
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DR EMBL; LMOZ01000002; KQR52507.1; -; Genomic_DNA.
DR RefSeq; WP_055919223.1; NZ_LMOZ01000002.1.
DR AlphaFoldDB; A0A0Q5LQL4; -.
DR STRING; 1736341.ASF88_13345; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000050966; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000050966}.
FT DOMAIN 415..589
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 56..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 674..701
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 70..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..210
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 424..431
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 474..478
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 528..531
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 922 AA; 96218 MW; ABBFB7ACACF395D0 CRC64;
MAAKPRVHEV ASELGVDSKV ALAKLKEMGE FVKGPSSSIE PPVARKLRAA LEAEGFTADK
ATAAPKAEAP RPAAPRPQGS SEPGAPKPQA PMSVAERQAA AEKAAADKAA AEKAAAETAA
PAAAAAAAPS EKAAPSAPRP GGATPAAGSI PRPGAPRPGN NPFSSSQGMG QRPSTPRPGN
NPYSSSQGMG QRPSPGNIPR PAPPRPGSPR IGAPGQGGGN RPGQRQGGGG GRPGFQQRPG
GAGGGAGGGF QRPGGGTGGG FGAPRPAGGG GRGRGPGGGT AGAFGRGGGK SKARKSKRAK
RQEFEMREAP SLGGVSVPRG DGGTVIRLRR GSSISDFADK IDANPASLVT VLFHLGEMAT
ATESLDEATF QILGEELGYK IQVVSPEDED RELLEGFDID LDAELEGESD EDLEIRPPVV
TVMGHVDHGK TRLLDAIRNA NVVAGEAGGI TQHIGAYQVW TEHEGIERAI TFIDTPGHEA
FTAMRARGAQ VTDIAILVVA ADDGIMPQTI EALNHAQAAN VPIVVAVNKI DKPEANPAKV
RQQLTEFGLV AEEYGGDVMF VDVSARNDIG IQDLLDAVLL TADAGLDLRA NPNKDARGVA
IEAKLDKGRG AVATVLIQSG TLRVGDAIVA GTAYGRVRAM ADENGDPVLE AAPSRPVQVQ
GLSSVPRAGD TFLVTEEDRT ARQIAEKREA AERNAQLAKA RKRISLEDFT RALEEGKVEA
LNLIIKGDVS GAVEALEESL MKIEVDDSVS LRILHRGVGA ITESDIDLAT IDNAIVIGFN
VRPDVKARER AAREGVDVRF YSVIYNAIED IENSLKGMLK PEFEEVQSGV AEIREVFRSS
KFGNIAGVIV RSGTITRNAK ARVIRDGVVV GDNLAIESLR RFKDDVTEVR TDFEAGIGLG
KYNDIQVGDE IETTELREKP RV
//
