ID U9VKR6_9CYAN Unreviewed; 695 AA.
AC U9VKR6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Elongation factor G {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:ESA33279.1};
GN ORFNames=N836_21565 {ECO:0000313|EMBL:ESA33279.1};
OS Leptolyngbya sp. Heron Island J.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA33279.1, ECO:0000313|Proteomes:UP000017515};
RN [1] {ECO:0000313|EMBL:ESA33279.1, ECO:0000313|Proteomes:UP000017515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Heron Island J {ECO:0000313|EMBL:ESA33279.1,
RC ECO:0000313|Proteomes:UP000017515};
RX PubMed=24503993;
RA Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA Fromme P.;
RT "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL Genome Announc. 2:e01166-e01113(2014).
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:ESA33279.1}.
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DR EMBL; AWNH01000103; ESA33279.1; -; Genomic_DNA.
DR RefSeq; WP_023075749.1; NZ_AWNH01000103.1.
DR AlphaFoldDB; U9VKR6; -.
DR STRING; 1385935.N836_21565; -.
DR PATRIC; fig|1385935.3.peg.5969; -.
DR eggNOG; COG0480; Bacteria.
DR OrthoDB; 580826at2; -.
DR Proteomes; UP000017515; 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: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:SF5; ELONGATION FACTOR G 1; 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:UP000017515}.
FT DOMAIN 5..280
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 78..82
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 132..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 695 AA; 76438 MW; 1324EC7BC7D99B52 CRC64;
MKDLSTYRNI GIFAHVDAGK TTTTERILNL TGKVHKIGEV HDGAATTDFM DQEKERGITI
QSAATSCFWN DHQLNIIDTP GHVDFTIEVY RSLKVLDGGI GVFCGSGGVE PQSETNWRYA
NDSEVARIIY VNKLDRTGAD FYRVVGQVKN VLAANPLVMV LPIGIENDFV GVVDLLTEKA
WIWDDSGEPM NYEIKDVPAD MTDEVAEWRE KLIEAAVEQD DDIMEKYLEG EELSIDEIKA
CIRKGTRELA FFPTYCGSSF KNKGVQLVLD AVVDYLPAPT EVKPQPEVDL EGNETGELAY
VDPEKPLRAL AFKIMDDRFG ALTFTRIYSG TLKKGDTILN TATGKSERVS RIVEMHADDR
QEMDAAQAGD IVALLGMKTV QTGHTLCDPK NPATLEPMVF PDPVISIAVE TKKKGESEKM
GIALSKMVQE DPSFQVETDQ ESGEIILKGM GELHLDIKVD ILKRTHGIEV EVGKPQVAYR
ESITKVLQDS YTHKKQSGGS GQYGKIDYII EPNETGAGFE FTSKVTGGNV PREFWPAVEK
GFAASMEKGM LAGFPVVDFK VTLTDGGFHP VDSSAIAFEI AAKAGYRQSF SKAGPQILEP
IMMVDVFAPE DYVGDVIGDL NRRRGMILGQ DVGPTGVRIK ADVPLSEMFG YIGDLRTMTS
GRGQFSMSFE KYSPCPKNVA EEVIKEAKER QGVAA
//
