ID A0A0B8ZWB0_9SPHN Unreviewed; 770 AA.
AC A0A0B8ZWB0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 ECO:0000313|EMBL:KHS42556.1};
GN ORFNames=NJ75_04117 {ECO:0000313|EMBL:KHS42556.1};
OS Novosphingobium subterraneum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=48936 {ECO:0000313|EMBL:KHS42556.1, ECO:0000313|Proteomes:UP000031338};
RN [1] {ECO:0000313|EMBL:KHS42556.1, ECO:0000313|Proteomes:UP000031338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12447 {ECO:0000313|EMBL:KHS42556.1,
RC ECO:0000313|Proteomes:UP000031338};
RA Gan H.M., Gan H.Y., Savka M.A.;
RT "Draft genome sequence of Novosphingobium subterraneum DSM 12447.";
RL Submitted (OCT-2014) 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:KHS42556.1}.
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DR EMBL; JRVC01000028; KHS42556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B8ZWB0; -.
DR STRING; 48936.NJ75_04117; -.
DR PATRIC; fig|48936.3.peg.4146; -.
DR Proteomes; UP000031338; 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; 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 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}.
FT DOMAIN 269..439
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 19..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 278..285
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 325..329
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 770 AA; 83038 MW; 3D4365829D33A750 CRC64;
MQARLLREAE EARLAALEAA NRREQEEKLK AIEEERRRAE EKAKAEAAPA PAPEPTPEPE
AAPTPAPTPV ATPEVAKQPE AAPAPVEAKA AEPKAEEAAP VIPAPRRFTP VASPAPIKRP
EPAAKKPAAN PRDRKTEDRR GGKLTVTRAL NEDEGARARS LAALKRAREK ERRAHFAGQS
QPREKQVRDV VVPDAITVQE LANRMAEKAA DLVKALFKMG MMVTINQTID QDTAELLVTE
FGHNIQRVSD SDADIDTSSD VDAEDTLQAR PPVVTIMGHV DHGKTSLLDA LRGTDVVRGE
AGGITQHIGA YQIKTKGGEF ITFLDTPGHE AFTEMRMRGA NVTDIVILVV AGDDGLMPQT
IEAINHTKAA GVPMIVAITK SDKPEFNPQK IRERLLEHEI IVEAMSGDVQ DVEVSAKSGA
GLDELIEKIL LQAELLELKA NPDRAAEATV IEAKLDKGKG PLATVLVNRG TLKVGDILVV
GTQSGRVRAM LDDKGRQVKA AGPSLPVEVL GIGGVPMAGD TLTVVESEAR AREVAAYRQE
RATAKRTVQA PASLENMFSA LAAKNTVIEY PLVVRADVQG SVEAIVNALN KISTDEIKVR
ILQSGVGAIT EGDVNLAQAS GAPIVGFNVR PNAKARELIE RNKVRMKYFD VIYQLTDDIR
SEMAGELGPE AIETVVGRAE VKEVFPAGKK DKAAGLLVVE GVIRKGLHAR LTRSDVIVSR
TTIASLRRFK DDVPEVRAGL ECGVLLQDTN DIKAGDQLEV FEVEMRDRTL
//
