ID W2UZB1_9RICK Unreviewed; 704 AA.
AC W2UZB1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Elongation factor G {ECO:0000256|ARBA:ARBA00017872, ECO:0000256|HAMAP-Rule:MF_00054};
DE Short=EF-G {ECO:0000256|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000256|HAMAP-Rule:MF_00054,
GN ECO:0000313|EMBL:ETO91190.1};
GN ORFNames=P857_680 {ECO:0000313|EMBL:ETO91190.1};
OS Candidatus Xenolissoclinum pacificiensis L6.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Xenolissoclinum.
OX NCBI_TaxID=1401685 {ECO:0000313|EMBL:ETO91190.1, ECO:0000313|Proteomes:UP000018951};
RN [1] {ECO:0000313|EMBL:ETO91190.1, ECO:0000313|Proteomes:UP000018951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L6 {ECO:0000313|Proteomes:UP000018951};
RX PubMed=24324632;
RA Kwan J.C., Schmidt E.W.;
RT "Bacterial endosymbiosis in a chordate host: long-term co-evolution and
RT conservation of secondary metabolism.";
RL PLoS ONE 8:E80822-E80822(2013).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome. {ECO:0000256|HAMAP-
CC Rule:MF_00054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00054}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000256|ARBA:ARBA00005870, ECO:0000256|HAMAP-
CC Rule:MF_00054}.
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:ETO91190.1}.
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DR EMBL; AXCJ01000008; ETO91190.1; -; Genomic_DNA.
DR AlphaFoldDB; W2UZB1; -.
DR STRING; 1401685.P857_680; -.
DR PATRIC; fig|1401685.3.peg.815; -.
DR Proteomes; UP000018951; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01886; EF-G; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR CDD; cd04088; EFG_mtEFG_II; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR047872; EFG_IV.
DR InterPro; IPR035649; EFG_V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004540; Transl_elong_EFG/EF2.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR NCBIfam; TIGR00484; EF-G; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00054};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00054}; Reference proteome {ECO:0000313|Proteomes:UP000018951}.
FT DOMAIN 14..294
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 23..30
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 92..96
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 146..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 704 AA; 78354 MW; C07E1A9671BD4C2B CRC64;
MSAIGESVSD IEMKVIRNIG IMAHIDAGKT TTTERILHYT GVEDRIGEVH DGNAVMDWMP
QERERGITIT SAATTCFWST ALMGKVRINI IDTPGHVDFT VEVERSLRVL DGAVAVFDGV
AGVEPQTETV WRQADKYNVP RICFVNKMDR MGVDFFRCVD MIGERLVAKA LVINLPIGSE
KDFVGVVDLI RMQAVVWKDE KMGAKYSYQD IPGDMLESAK RYREMMMDEL SLIDEDIMNK
YLEGEEVSEE ILKSAIRAGV RDGSFYPVLC GSAFKNKGVQ TLLDAIVDYL PSPVDMGDVN
LVSQEDGFVL KPSSDGMLSA LAFKVANDPF VGTLTYMRIY SGTLNSSSNL YNLTKGKKER
VGRMVLMHSN SREDIKRIKA GNIVAVPGLK YTTTGDTLSD SKDADFLLES MDFPMGVIET
ALEPKTKVDQ EKMSVALSRL SREDPSLQVK VDEETGQTII KGMGELHLEI IVDRLLRDFQ
VEVNCGEPKV AYRETIKERV DVEYLHKKQT GGAGQYAEVK MIFEPYVLGE DDSSGYVFEN
KIVGGAVPKE YIPGVVKGIE YMKDTGVLAG YPVINFKVTL YDGSAHDVDS SSYAFEAAVK
GCFRKILDKM ILLEPIMNLE VMVPEDYLGD VVGDLNGARS GKIIDMRDER GMKVIQAEVP
LSKMMGYSNP LRSMTQGRAN FTMSFKAYEK VPDYESLEII KRNS
//
