ID A0A0C1DH07_9SPHI Unreviewed; 1023 AA.
AC A0A0C1DH07;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, 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=OC25_14285 {ECO:0000313|EMBL:KIA93195.1};
OS Pedobacter kyungheensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1069985 {ECO:0000313|EMBL:KIA93195.1, ECO:0000313|Proteomes:UP000031246};
RN [1] {ECO:0000313|EMBL:KIA93195.1, ECO:0000313|Proteomes:UP000031246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 16221 {ECO:0000313|EMBL:KIA93195.1,
RC ECO:0000313|Proteomes:UP000031246};
RA Anderson B.M., Newman J.D.;
RT "Pedobacter Kyungheensis.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC {ECO:0000256|ARBA:ARBA00003987}.
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}.
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:KIA93195.1}.
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DR EMBL; JSYN01000016; KIA93195.1; -; Genomic_DNA.
DR RefSeq; WP_039477205.1; NZ_JSYN01000016.1.
DR AlphaFoldDB; A0A0C1DH07; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000031246; 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; 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; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
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 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}.
FT DOMAIN 522..692
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 73..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 531..538
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 578..582
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 632..635
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1023 AA; 110300 MW; 607449ABF853B3B3 CRC64;
MSDDKPIILI KAIKELNIGM GTAVEFLNKK GFSAEKSPMF KLTGEMYNAL LKEYQGDKIV
REEAKQIVIG KIRRDEPETE KPVEAPKKNT DFEKNEEILI KNAQSFTPPV EKPKVVETPK
VETPAPAPTP AAAAPVATPK AEEKAEEKAD ESALPGVKIV GKIDLNDLNS KTRPVKKEET
PAPAPVEKTP EPVKPVEQPK AEEKPVEVKK AETPAPAPVA AAPVAKAPEP VKPVEQPKAE
EKPADAKPAS SEPEVIKART VKLTGPNIIG KIVLPTTPDR RNGPVASSSD SEAAKRKRKR
KKTPGAPGQP GQHGGQGQQG QHPAGQGGAP GQPRQPYQGN RPGGGTPYQG NRPAGQGGTP
YQGNRNNNRP GFQNRNAAPS GPKEEPTEKE IQDQIKATLA RLSGAGKSGK FAQRAKLRRQ
KRDDVASNAE EAANELESQS KILKVTEFVT ANELANMMDV PVTKIIGTCM SLGMFVSINQ
RLDAETLTIV ADEFGYEIQF VKPDEEEDNI IEEEDNEEDL IERAPVVTIM GHVDHGKTSL
LDYIRKANVV AGEAGGITQH IGAYMVTTPS GKKVTFLDTP GHEAFTAMRA RGAKAADIAI
IVIAADDAVM PQTKEAINHA QAAGVPLVFA FTKVDKPGAN ADKVREQLSV MNILVEDWGG
KYQSQEISSK SGLNVDLLLD KVLLEAELLE LKANPNKRAT GTVIESALDK GRGIVTTVLV
QGGTLKVGDP ILAGSYSGRV KALTNERGAK VDSAGPSQPV QVLGMQGAPT AGDRFNALES
ETEARDIANK RMQLQREQGL RTQKHITLDE IGRRLAIGNF KELNIIVKGD VDGSIEALSD
SLLKLSTEQI QINVISKGVG QISESDVLLA SASDAIIIGF QVRPSTGARK LAEAEQIDIR
LYSIIYDAIN EIKSAMEGML DPEFEEKIVA NVEIRETFKI TKVGTIAGCM VLDGKITRNS
KVRVVRDGVV IYTGELASLK RFKDDVKEVS KGYECGLNIQ NFNNIEVGDI VEAYEQVEVA
RKL
//
