ID K1UFM6_9ZZZZ Unreviewed; 639 AA.
AC K1UFM6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Tetracycline resistance protein TetM {ECO:0000313|EMBL:EKC78814.1};
GN ORFNames=LEA_03096 {ECO:0000313|EMBL:EKC78814.1};
OS human gut metagenome.
OC unclassified sequences; metagenomes; organismal metagenomes.
OX NCBI_TaxID=408170 {ECO:0000313|EMBL:EKC78814.1};
RN [1] {ECO:0000313|EMBL:EKC78814.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22891823; DOI=10.1111/j.1462-2920.2012.02845.x;
RA Ferrer M., Ruiz A., Lanza F., Haange S.B., Oberbach A., Till H.,
RA Bargiela R., Campoy C., Segura M.T., Richter M., von Bergen M., Seifert J.,
RA Suarez A.;
RT "Microbiota from the distal guts of lean and obese adolescents exhibit
RT partial functional redundancy besides clear differences in community
RT structure.";
RL Environ. Microbiol. 15:211-226(2013).
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:EKC78814.1}.
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DR EMBL; AJWY01002065; EKC78814.1; -; Genomic_DNA.
DR AlphaFoldDB; K1UFM6; -.
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; cd03711; Tet_C; 1.
DR CDD; cd03690; Tet_II; 1.
DR CDD; cd16258; Tet_III; 1.
DR CDD; cd01684; Tet_like_IV; 1.
DR CDD; cd04168; TetM_like; 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; IPR041095; EFG_II.
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 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 PRINTS; PR00315; ELONGATNFCT.
DR PRINTS; PR01037; TCRTETOQM.
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}.
FT DOMAIN 1..244
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 639 AA; 72475 MW; CA23D691DFE2B1B3 CRC64;
MKIINLGILA HVDAGKTTLT ESLLYTSGAI AELGSVDEGT TRTDTMNLER QRGITIQTAV
TSFQWEDVKV NIIDTPGHMD FLAEVYRSLS VLDGAVLLVS AKDGIQAQTR ILFHALQTMK
IPTIFFINKI DQEGIDLPMV YREMKAKLSS EIIVKQKVGQ HPHINVTDND DMEQWDAVIM
GNDELLEKYM SGKPFKMSEL EQEENRRFQN GTLFPVYHGS AKNNLGIRQL IEVIASKFYS
STPEGQSELC GQVFKIEYSE KRRRFVYVRI YSGTLHLRDV IRISEKEKIK ITEMCVPTNG
ELYSSDTACS GDIVILPNDV LQLNSILGNE MLLPQRKFIE NPLPMLQTTI AVKKSEQREI
LLGALTEISD GDPLLKYYVD TTTHEIILSF LGNVQMEVIC AILEEKYHVE AEIKEPTVIY
MERPLRKAEY TIHIEVPPNP FWASVGLSIE PLPIGSGVQY ESRVSLGYLN QSFQNAVMEG
VLYGCEQGLY GWKVTDCKIC FEYGLYYSPV STPADFRLLS PIVLEQALKK AGTELLEPYL
HFEIYAPQEY LSRAYHDAPR YCADIVSTQI KNDEVILKGE IPARCIQEYR NDLTYFTNGQ
GVCLTELKGY QPAIGKFICQ PRRPNSRIDK VRHMFHKLA
//
