ID A0A0N0KET4_9SPHN Unreviewed; 872 AA.
AC A0A0N0KET4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-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=IP81_11245 {ECO:0000313|EMBL:KPF91480.1};
OS Novosphingobium sp. AAP83.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523425 {ECO:0000313|EMBL:KPF91480.1, ECO:0000313|Proteomes:UP000037998};
RN [1] {ECO:0000313|EMBL:KPF91480.1, ECO:0000313|Proteomes:UP000037998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP83 {ECO:0000313|EMBL:KPF91480.1,
RC ECO:0000313|Proteomes:UP000037998};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-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:KPF91480.1}.
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DR EMBL; LJHY01000020; KPF91480.1; -; Genomic_DNA.
DR RefSeq; WP_054108084.1; NZ_LJHY01000020.1.
DR AlphaFoldDB; A0A0N0KET4; -.
DR STRING; 1523425.IP81_11245; -.
DR PATRIC; fig|1523425.4.peg.1643; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000037998; 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; 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; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
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:UP000037998}.
FT DOMAIN 371..539
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 66..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 380..387
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 427..431
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 872 AA; 93220 MW; A113AA34DFE5BF0C CRC64;
MSDSDKKPTL GRRPLGLKTA VEAGEVKQTF SHGRTNKVVV EVKRRKLVGR PGEAAPVAAP
VVAAPAPAPV AAPPPPPPPP PPPAASRETR QEMQTRLLRE AEEARLASAE ANNRREQEAR
LRALEEERRR SEEAARPAEP VVAAPAPEPV VAPAPPAAPE VATAEVTAPA PAPTPVAEPE
VAKAPEPAAK AAEEAPKAAE PAAIPAPRRF TPVASTAPAK RPEPAAKKPA GAPRDRKVED
RRGGKLTVTR ALNDDEGARA RSLAALKRAR EKEKRAHFAG QSQPREKQVR DVIVPDAITV
QELANRMAEK AADLIKALFK MGMMVTINQT IDQDTAELLV TEFGHNIERV SDSDADIDTT
TDVDDNESLA PRPPVVAIMG HVDHGKTSLL DALRGTDVVR GEAGGITQHI GAYQIKTKGG
DHITFLDTPG HEAFTEMRMR GANVTDIVIL VVAGDDGLMP QTIEAINHTK AAGVPMIVAI
TKSDKPEFNP QKIRERLLEH EILVEAMSGD VQDVELSAKT GAGLDELIEK ILLQAELLEL
GANPDRAADA TVIEAKLDKG KGPLATVLIN RGTLKVGDIL VVGTQSGRVR AMLDDKGRQI
KEAGPSLPVE VLGLGGVPMA GDTLTVVESE ARAREVAAYR QEMATAKRTV QAPVNLENMF
SALATKNAVI EYALVVRGDV QGSVEAIVNA LNKISTDEIK VRILSSGVGA ITESDVNLAQ
ASGAPIVGFN VRPNAKAREL IERNKVRMKY FDVIYQLTDD IRSEMAGELG PEAIETVVGR
AEVKEVFPAG KKDKAAGLLV VEGVIRKGLH ARLTRNDVIV SRTTISSLRR FKDDVAEVRG
GLECGVLLTD TNDIKAGDQL EVFEVEMRDR TL
//
