ID   GUFP_PAUCH              Reviewed;         602 AA.
AC   B1X3K4;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Translation factor GUF1 homolog, organellar chromatophore {ECO:0000255|HAMAP-Rule:MF_03138};
DE            EC=3.6.5.-;
DE   AltName: Full=Elongation factor 4 homolog {ECO:0000255|HAMAP-Rule:MF_03138};
DE            Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_03138};
DE   AltName: Full=GTPase GUF1 homolog {ECO:0000255|HAMAP-Rule:MF_03138};
DE   AltName: Full=Ribosomal back-translocase {ECO:0000255|HAMAP-Rule:MF_03138};
GN   Name=lepA {ECO:0000255|HAMAP-Rule:MF_03138}; OrderedLocusNames=PCC_0066;
OS   Paulinella chromatophora.
OG   Plastid; Organellar chromatophore.
OC   Eukaryota; Sar; Rhizaria; Imbricatea; Silicofilosea; Euglyphida;
OC   Paulinellidae; Paulinella.
OX   NCBI_TaxID=39717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA   Nowack E.C.M., Melkonian M., Gloeckner G.;
RT   "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT   photosynthesis by eukaryotes.";
RL   Curr. Biol. 18:410-418(2008).
CC   -!- FUNCTION: Promotes protein synthesis. May act as a fidelity factor of
CC       the translation reaction, by catalyzing a one-codon backward
CC       translocation of tRNAs on improperly translocated ribosomes.
CC       {ECO:0000255|HAMAP-Rule:MF_03138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03138};
CC   -!- SUBCELLULAR LOCATION: Plastid, organellar chromatophore.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. LepA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03138}.
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DR   EMBL; CP000815; ACB42523.1; -; Genomic_DNA.
DR   RefSeq; YP_002048733.1; NC_011087.1.
DR   AlphaFoldDB; B1X3K4; -.
DR   SMR; B1X3K4; -.
DR   GeneID; 6481284; -.
DR   GO; GO:0070111; C:organellar chromatophore; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   CDD; cd03709; lepA_C; 1.
DR   Gene3D; 3.30.70.2570; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_03138; GUFP; 1.
DR   HAMAP; MF_00071; LepA; 1.
DR   InterPro; IPR006297; EF-4.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027518; GUFP.
DR   InterPro; IPR038363; LepA_C_sf.
DR   InterPro; IPR013842; LepA_CTD.
DR   InterPro; IPR035654; LepA_IV.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR43512; PTHR43512; 2.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF06421; LepA_C; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR01393; lepA; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Hydrolase; Nucleotide-binding; Organellar chromatophore;
KW   Plastid; Protein biosynthesis.
FT   CHAIN           1..602
FT                   /note="Translation factor GUF1 homolog, organellar
FT                   chromatophore"
FT                   /id="PRO_0000402922"
FT   DOMAIN          7..189
FT                   /note="tr-type G"
FT   BINDING         16..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
FT   BINDING         82..86
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03138"
SQ   SEQUENCE   602 AA;  67114 MW;  2442CB46379C4B57 CRC64;
     MTDAPLSRIR NFCIIAHIDH GKSTLADRLL QDTGTVAARD MQEQFLDNME LERERGITIK
     LQAARMEHIA NDGEAYILNL IDTPGHVDFS YEVSRSLQAC EGALLVVDAS QGVEAQTLAN
     VYLALEQNLE IIPVLNKIDL PGADPERVRQ EIEAIIGLDT SKAITCSAKT GIGISEILQA
     IVERIPPPVD AIEEPLKALI FDSYYDPYRG VIVYFRVMSG QIKTRDKILL MASKKNYELD
     EVGIMIPGER KVDSLHAGEV GYLAASIKSV ADARVGDTIT LANNPANNAL PGYTEVKPVV
     FCGLFPTDAD QYPDLREALA RLQLSDAALK YEPETSSAMG FGFRCGFLGL LHMEIVQERL
     EREYDLDLIV TAPSVVYKVN MIDESTVMVD NPATLPGPQK RKSIEEPYVK LEIYTPNSYN
     GTLMELCQER RGEFIDMKYL TTDRVTLHYE LPLAEVVTDF FDQMKSRTKG YASMEYNLIG
     YRPNDLVCLD ILINNEKADP LTTIVHRDKA YNVAKGLVEK LKELIPRQQF KIPLQASIGS
     RVIASESISA IRKDVLAKCY GGDISRKKKL LQKQAKGKKR MKAMGKVDVP QEAFMAVLTL
     NK