ID A0A0P1LN10_9BACT Unreviewed; 947 AA.
AC A0A0P1LN10; A0A0P1MPC5; A0A0P1P1C0; A0A0S4MRM0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=JGI4_00325 {ECO:0000313|EMBL:CUU01642.1};
OS Candidatus Kryptonium thompsoni.
OC Bacteria; Candidatus Kryptonia; Kryptonium.
OX NCBI_TaxID=1633631 {ECO:0000313|EMBL:CUU01642.1, ECO:0000313|Proteomes:UP000182011};
RN [1] {ECO:0000313|EMBL:CUU01642.1, ECO:0000313|Proteomes:UP000182011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JGI-4 {ECO:0000313|EMBL:CUU01642.1};
RA Zhang Y., Guo Z.;
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 ECO:0000256|RuleBase:RU000645}.
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; FAOP01000002; CUU01642.1; -; Genomic_DNA.
DR RefSeq; WP_047133898.1; NZ_CZVX01000034.1.
DR AlphaFoldDB; A0A0P1LN10; -.
DR STRING; 1633631.GCA_001442925_00327; -.
DR Proteomes; UP000182011; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
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.
DR PROSITE; PS01176; IF2; 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:UP000182011}.
FT DOMAIN 440..610
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 50..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 333..365
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 94..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 449..456
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 496..500
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 550..553
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 947 AA; 107049 MW; 8399481BC5FF8DC4 CRC64;
MPKRIYQIAK ELNISSDELV SFLQKQGFDV KGYMSPVDDK MLEIINKHYK HEREQAERQK
RKREKEAREV KPAKVEPRTV VEEIETKLPA EQKEVEPTQV VKIEAEEPKP EFVQPAEEVA
VQGSEPVTAE EKSAEIAVSE IKEAKDETKD KVEQVEELAQ KQAETVIEEH AEAKGETAEL
KEAPAKPEEK QAEPVGSEKA TGMVYVKVEE RKEFRKDDRR KRFEAERERD RRRERRRGKR
RKEFREEKPV KEETTVSDVI HAPEVEAIKE ETRKRKQIKE KEEKKRKIVE IDDFEIKKPL
KRKKSRIEID EAEILRNIDQ TLAEMEDSGP DIREIIKKRK KKERQEKEEK KVEQIEREKR
KIKVAEFITV NELANIIGVS ASEIIKKCLN LGLVVSINQR LDFDTITLIA SDYGFEVERA
EEYLEDIIEE EPDHPEDLEP RPPVVTIMGH VDHGKTTLLD YIRQSNIVAG EAGGITQHIG
AYQVTLPNGK QITFIDTPGH EAFTAMRARG AQVTDIVVLV VAADDAVMPQ TVEAINHALA
ANVPIIVAIN KIDKPGANPD KIKQQLAERG ILVEDWGGKY QCVEISAKYG KNVDLLLEKI
LLEAELMELK ANPKKRARGV VIESKLDKGR GPVGTVLVQT GTLKIGDPFV AGTTFGRVRA
MFDERGNRVE IAKPSTPVQV IGFDQLPEAG DSFIVVEDEK RAREIANRRA QLKREQTFRQ
LRAVSLNKLS EQIKEGKVKE LPIIIKADVN GSVEALSDSL MKLSTEEVKV RIIHRAVGAI
SESDVLLAQA SGAIIIGFNV RPTSGAKKLA ESENVEIRLY NIIYNVIEDV KKALEGMLEP
ERREEFLGTA EVREVFKISK VGTVAGCFVT EGKILRSARA RLIRNGIVIY DGKIASLKRF
KDDVKEVEAG LECGVALENY NDIKVGDVIE AYNILEIKRK LEEVKGS
//
