ID A0A150XHE4_9BACT Unreviewed; 942 AA.
AC A0A150XHE4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=AWW68_05005 {ECO:0000313|EMBL:KYG78129.1};
OS Roseivirga spongicola.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC Roseivirga.
OX NCBI_TaxID=333140 {ECO:0000313|EMBL:KYG78129.1, ECO:0000313|Proteomes:UP000075606};
RN [1] {ECO:0000313|EMBL:KYG78129.1, ECO:0000313|Proteomes:UP000075606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UST030701-084 {ECO:0000313|EMBL:KYG78129.1,
RC ECO:0000313|Proteomes:UP000075606};
RA Selvaratnam C., Thevarajoo S., Goh K.M., Ee R., Chan K.-G., Chong C.S.;
RT "Genome sequencing of Roseivirga spongicola UST030701-084.";
RL Submitted (JAN-2016) 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:KYG78129.1}.
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DR EMBL; LRPC01000001; KYG78129.1; -; Genomic_DNA.
DR RefSeq; WP_068217253.1; NZ_LRPC01000001.1.
DR AlphaFoldDB; A0A150XHE4; -.
DR STRING; 333140.AWW68_05005; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000075606; 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; IPR028626; Ribosomal_eS28_CS.
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 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.
DR PROSITE; PS00961; RIBOSOMAL_S28E; 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}; Reference proteome {ECO:0000313|Proteomes:UP000075606}.
FT DOMAIN 441..611
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 58..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 450..457
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 497..501
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 551..554
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 942 AA; 104038 MW; 3D7EE10F509A1058 CRC64;
MSEEKMMRLS QVARKLNVGR NTIVDFLSAK GFSVDSSPNA KISSEQYDML AKEFAASAHE
KEEASHLTIG TKHVEDMVID SSGVTTEPKK EPAKKEEPKP APTPPPTPEE NKVEEKKPEP
EVKPEAEKPK EAPKEEPKKE PAKKEEPAPE AESKPEAAPK AKEVEQKKEE EKPEEEKKTG
LRVLGKIDLN KGKKKEEKPK QQPKKEEKKA EAPKKEEPAK PAEPEKYQAK ADSLRGLKVL
GKIELPTEKP KKSKDDDKDK KGGDQRGKRP RKRIQQTKVE RANKGSNDNR RGGNQNRGRR
PAPKEELTDK EIQEQIKETL ARLSGGSKGG GKNRSKYRKE KRSAAAEAAE EEMLRQQEES
KILKVTEFIS ASDLASLMNV SVNEVISTCM SLGMFVSINQ RLDAEAITII SDEFGYDVQF
TSADDEVDVV EEEDKEEDLQ ERAPIVTIMG HVDHGKTSLL DYIREANVTA GEAGGITQHI
GAYDVETKDG KRIAFLDTPG HEAFTAMRAR GAKITDVAII VVAADDNVMP QTKEAINHAQ
VAEVPIVIAI NKVDKPTANP DKIREELANL NILVEDWGGK YQCQEVSAKT GQGIEELLEK
VLLEAELLEL KANPDKSGVG TVVEASLDKG RGYLATLMVQ SGTMKVGDVV LAGSHYGKVK
AMFDHRGNRL KVVGPSTPVQ MLGLDGAPQA GDRFNVMESE REAREIANKR EQILREQSVR
TKKHITLDEI GRRLAVGNFK ELNVIVKGDV DGSVEALSDS LLKLSTEEVQ VNIIHKAVGQ
ISESDVLLAT ASDAVILGFQ VRPSGGARRL AENEEIEIRL YSIIYDAINE IKDAMEGLLE
PTEKEVITGN IEVRETFKIS KVGTVAGCYV TEGFVKRQNQ IRLIRDGIVV YTGDIGQLKR
FKDDVNEVKS GYECGLSIKN FNDIKVGDVI EGFEIQEVKR TL
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