ID A0A1R3WJL3_9MICO Unreviewed; 933 AA.
AC A0A1R3WJL3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN05880545_1846 {ECO:0000313|EMBL:SIT78088.1};
OS Microbacterium sp. RU33B.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1907390 {ECO:0000313|EMBL:SIT78088.1, ECO:0000313|Proteomes:UP000187047};
RN [1] {ECO:0000313|EMBL:SIT78088.1, ECO:0000313|Proteomes:UP000187047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU33B {ECO:0000313|EMBL:SIT78088.1,
RC ECO:0000313|Proteomes:UP000187047};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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}.
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DR EMBL; FTPO01000001; SIT78088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3WJL3; -.
DR STRING; 1907390.SAMN05880545_1846; -.
DR Proteomes; UP000187047; 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}; Reference proteome {ECO:0000313|Proteomes:UP000187047}.
FT DOMAIN 426..600
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 50..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..133
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..220
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 435..442
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 485..489
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 539..542
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 933 AA; 96368 MW; 8F06A72AED036B07 CRC64;
MANAKPRVHE IASELGVDSK VALAKLKELG EFVKSPSSTI EPPVARKLRA ALEADGASQS
AEKPAAPAAA RPAAPARPGA RPGPARPAAP AATPAPAPAA PAPAPAAAAP AAPAPAAPAP
AAPAAPAPAP AAPAAPAAAQ STGDGGATPA APRPGGAPRP GNNPFASAQG MGQRPAGPRP
GNNPFASAQG MGQRPSPTPG NIPRPQAPRP GAPRPGAPRP GGAGRPGGGG RPGAPFQQRP
GGPGRPGGAG GGFQRPGGAP GGAPAGGFAG RPGGGGGRGR GPGGGTAGAF GKGGGKSKQR
KSRRAKRQEF EMRSAPVVGG VNVSRGNGEI IRMRRGASIA DFADKIEAIT GYTVQPGTLV
TILFNLGEMA TATESLDEAT FEVLGAELGY KIQMVSPEDE DKELLEGFGL DLEAELEAES
EDDLEIRPPV VTVMGHVDHG KTRLLDAIRK TNVVAGEAGG ITQHIGAYQV WTEHDGIERA
ITFIDTPGHE AFTAMRARGA QVTDLAILVV AADDGIMPQT VEALNHAQAA NVPIVVAVNK
VDKPDANPAK VRQQLTEYGL VAEEYGGDVL FVDVSARDGL GIQELLDAVL LTADAGLDLT
ANPNKAARGV AIEAKLDKGR GSVATVLIQS GTLRVGDAIV AGTAYGRVRA MADENGDPVL
EAWPSRPVQV QGLNSVPRAG DTFIVTDEDR LARQIAEKRE AAERNAQLAK ARKRISLEDF
TRALQEGKVE SLNLIIKGDV SGAVEALEES LLKIEVDDSV QLRIIHRGVG AITESDVNLA
TIDNAIIIGF NVRPDTKARE RASREGVDTR FYSVIYNAID DVEQSLKGML KPEYEEVQSG
VAEIREVFRS SKFGNIAGVI VRSGTITRNA KARVIRDGVV LADGLAIESL RRFKDDVTEV
RTDYEAGIGL GKYNDIQVGD EIETTELIEK PRG
//
