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Database: UniProt
Entry: A0A1N6F475_9LACT
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ID   A0A1N6F475_9LACT        Unreviewed;       695 AA.
AC   A0A1N6F475;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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   ORFNames=SAMN05878443_0388 {ECO:0000313|EMBL:SIN90065.1};
OS   Carnobacterium alterfunditum.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=28230 {ECO:0000313|EMBL:SIN90065.1, ECO:0000313|Proteomes:UP000184758};
RN   [1] {ECO:0000313|EMBL:SIN90065.1, ECO:0000313|Proteomes:UP000184758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=313 {ECO:0000313|EMBL:SIN90065.1,
RC   ECO:0000313|Proteomes:UP000184758};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FSRN01000001; SIN90065.1; -; Genomic_DNA.
DR   RefSeq; WP_034546946.1; NZ_FSRN01000001.1.
DR   AlphaFoldDB; A0A1N6F475; -.
DR   STRING; 28230.SAMN05878443_0388; -.
DR   eggNOG; COG0480; Bacteria.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000184758; 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: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}.
FT   DOMAIN          9..283
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT   BINDING         82..86
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   695 AA;  76380 MW;  D3708C0EBA0560FF CRC64;
     MAKREFSLNN TRNIGIMAHI DAGKTTTTER VLYYTGKIHK IGETHEGASQ MDWMEQEQER
     GITITSAATT AAWKGYRVNI IDTPGHVDFT VEVERSLRVL DGAVALLDAQ SGVEPQTETV
     WRQATTYGVP RIVFVNKMDK TGADFIYSVG TILDRLQANA HPIQLPIGAE DNFTGIIDLV
     TMKAEVYTND LGTDIREEEI PEEYVELANE WRTKLIEGAA DTDEALMEKY LDGEEISEEE
     LKNAIRKATL KVEFYPVLCG SAFKNKGVQM MLDAVIDYLP SPLDVAAIQG ILPDSEETAE
     RHADDSEPFS ALAFKVMTDP YVGRLTFFRV YSGTLQAGSY VQNSTKGKRE RVGRILQMHA
     NSRSEIPEVF AGDIAAAVGL KNTTTGDTLC DEKDQVILES MDFPEPVIQV AIEPKSKADQ
     DKMGVALQKL AEEDPTFRAE TDHETGETII AGMGELHLDI IVDRMRREFN VEASVGAPQV
     SYRETFRGST KAEGKFVRQS GGKGQYGHVW IEFSPNEEGK GFDFEDAIVG GTVPREYIPA
     VKAGLEASLN NGVLAGYPLV DIKAKLYDGS YHDVDSNETA FKVAASMALK NASKKANPVI
     LEPMMGVEIT IPEDYLGDVM GHISARRGRI EGSEARGNTT IVKGMIPLAE MFGYATALRS
     ATQGRGTFSM TFDHYEDVPK SISEEIIKKN GGSAN
//
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