ID A0A249KHG5_9ACTN Unreviewed; 900 AA.
AC A0A249KHG5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=A1sIA56_04425 {ECO:0000313|EMBL:ASY16145.1};
OS Candidatus Planktophila sulfonica.
OC Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC Candidatus Nanopelagicaceae; Planktophila.
OX NCBI_TaxID=1884904 {ECO:0000313|EMBL:ASY16145.1, ECO:0000313|Proteomes:UP000217215};
RN [1] {ECO:0000313|EMBL:ASY16145.1, ECO:0000313|Proteomes:UP000217215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-IA-56 {ECO:0000313|EMBL:ASY16145.1};
RA Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT "High microdiversification within the ubiquitous acI lineage of
RT Actinobacteria.";
RL Submitted (JUL-2016) 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; CP016773; ASY16145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249KHG5; -.
DR KEGG; psuf:A1sIA56_04425; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000217215; Chromosome.
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 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:UP000217215}.
FT DOMAIN 396..570
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 53..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 405..412
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 455..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 509..512
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 900 AA; 94392 MW; 2196C11A01AD6A68 CRC64;
MSKVRVHELA KQLGMESKEV LAKLQEMGEF VRSASSTVEA PVVRKLVALY PDAKPAEDKK
PVKKAAAKKT AASKKTAEVN PELAAELAAE LGVDLAALKA SRDAEKIAQE EAKAAASEAT
SAESTPAPGA TPATPAAPRP GNNPFSTGGA VPRPPRPGNN PFSAGGAVPR PPAQRPGAPR
PGMAGARPGS VRPGFAARPG APRPAGAGTG TGNYPPRTGG APSSGPYRSQ GAPGAGGTAG
GPQRPGGGGP NRGPGRGGTA GAFGKNASKS SKRKQKSRKA LREEFDNMQA PQLGGAVIPH
GDGKTKIRMR RGASLADFAE KIGADPAALV SALFHLGEMV TATQSVDADT FEILGAQLKY
QIEIVSPEDE DRELLQDFDI DLAQELEDMN PDDLVARPPV VTVMGHVDHG KTSLLDAIRK
TEVIKGEAGG ITQHIGAYQI HHDHDGVNRA ITFIDTPGHE AFTAMRARGA KVTDIAVLVV
AADDGIMPQT IEALNHAQAA DVPIVVAVNK VDKEGANPDK VRQQLTEYNL IAEEYGGDTI
FVNVSAKKGE GVDALIDSIL LTADAAIDLR AIAADDARGV AIEAHLDRGR GPVATVLVQR
GTLKIGDAIV AGGSFGRVRA MLDEHGANVE EAGPSRPVQV LGFTSVPNAG DTFLVAEDDR
TARQIAEKRQ AAERNAQLAK ARKKVSLEDF MEQSKISTLN LILKGDVSGS VEALEDALMQ
LDVGAEVDLR VIHRGVGAIT KSDITLASAS TAVVIGFNVK PEPQTAIFAD QEGVEVRFYS
VIYNAIEEIE LSLKGLLKPE YEEVILGNAE VRDLFKSSKV GTIAGSIVTD GIIRRNAKGR
VLRHGAVLAE DVTIESLKRF KDDATEVKEG FECGIGVGKG ADLQVGDIIQ VFEMREKKRA
//
