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Database: UniProt
Entry: R5SQP7_9CLOT
LinkDB: R5SQP7_9CLOT
Original site: R5SQP7_9CLOT 
ID   R5SQP7_9CLOT            Unreviewed;       870 AA.
AC   R5SQP7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Small GTP-binding protein domain {ECO:0000313|EMBL:CCZ53164.1};
GN   ORFNames=BN771_01569 {ECO:0000313|EMBL:CCZ53164.1};
OS   Clostridium sp. CAG:75.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262836 {ECO:0000313|EMBL:CCZ53164.1, ECO:0000313|Proteomes:UP000018032};
RN   [1] {ECO:0000313|EMBL:CCZ53164.1, ECO:0000313|Proteomes:UP000018032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:75 {ECO:0000313|Proteomes:UP000018032};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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   -!- 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:CCZ53164.1}.
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DR   EMBL; CBAE010000263; CCZ53164.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5SQP7; -.
DR   Proteomes; UP000018032; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   CDD; cd10912; PIN_YacP-like; 1.
DR   CDD; cd03711; Tet_C; 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   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
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; IPR035650; Tet_C.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   InterPro; IPR010298; YacP-like.
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; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF05991; NYN_YacP; 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   4: Predicted;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018032}.
FT   DOMAIN          1..227
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   870 AA;  98783 MW;  1C50BD1AAC0E69AF CRC64;
     MKHITIGILA HVDAGKTTLS EGLLYTAGSI RQLGRVDDQN AFLDNNHMER DRGITIFSKP
     ARFALQDGTV TLLDTPGHVD FSAEMERALQ VLDYAVLVVS AADGVQSHTE TLWQLFAYYD
     IPVFLFINKM DMPDTDRGRI MQELQEKLSD ACVDFMAEPE SVMEAAAMCE EDLLERFLQD
     GTLEDADVIR LIRQRKLFPC YFGSALKMQG VETFLKGLWQ YTEPGQYGDE FGARVYKISR
     DEQGNRLTHL KVTGGRLQAR QLLQGKKQLQ SDDGDEEQIW SEKINQIRFY SGEKYTTAKE
     AKAGEICAVT GLSHTYPGEG LGFMEHDEVP ILEPVLTYRI FLEPDWDVRR ALPLLKQLEE
     EEPELHIIWD ETLKELHAQV MGEVQIEVIR QQLFDRYRMH VTFGEGNIVY KETIAAPVIG
     MGHFEPLRHY AEVHLLLEPG EPESGLVFDT NCSEDMLSKN WQRLILTHLQ EKKHRGVLTG
     SEITDMRISV IAGKAHVKHT EGGDFRQATY RAVRQGLRQA ETILLEPYYS FRLELPTEQL
     GRAMTDMERM SAKLNAPDSS GEYAVLAGEA PVATIRSYQK DLSAYTGGKG KMSCQLCGYR
     PCHNTEEVVA QIGYDPDLDY AATADSVFTA HGSGYIVPWN EVADHVHVDN GYSLEGKQSP
     EDDYAEPMTA AMRRRRRYDT EYSMGEEEIR SILGQAGGAN RNQKKNWIRQ RKRVVSSTDS
     RGPVAYKRSA EKYLLVDGYN IVFAWDELNE LAKDNIDAAR DRLMDILCNY QAYMGMTLIL
     VFDAYKVKGG IGQMLDYHNI HVVYTKEAET ADQYIEKLAH NMGREHDVTV ATSDGLEQLI
     IRGQGCKLWS AREFYAEVKR VEEAIRRQVE
//
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