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Database: UniProt
Entry: A0A1M3GJ74_9PROT
LinkDB: A0A1M3GJ74_9PROT
Original site: A0A1M3GJ74_9PROT 
ID   A0A1M3GJ74_9PROT        Unreviewed;       325 AA.
AC   A0A1M3GJ74;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Tellurium resistance protein TerC {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BGO60_07640 {ECO:0000313|EMBL:OJW41606.1};
OS   Thiobacillus sp. 65-1059.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=1895860 {ECO:0000313|EMBL:OJW41606.1, ECO:0000313|Proteomes:UP000184230};
RN   [1] {ECO:0000313|EMBL:OJW41606.1, ECO:0000313|Proteomes:UP000184230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=65-1059 {ECO:0000313|EMBL:OJW41606.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the TerC family.
CC       {ECO:0000256|ARBA:ARBA00007511}.
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:OJW41606.1}.
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DR   EMBL; MKUE01000139; OJW41606.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3GJ74; -.
DR   STRING; 1895860.BGO60_07640; -.
DR   Proteomes; UP000184230; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR005496; Integral_membrane_TerC.
DR   InterPro; IPR022369; Integral_membrane_TerC_rswitch.
DR   NCBIfam; TIGR03718; R_switched_Alx; 1.
DR   PANTHER; PTHR30238; MEMBRANE BOUND PREDICTED REDOX MODULATOR; 1.
DR   PANTHER; PTHR30238:SF0; THYLAKOID MEMBRANE PROTEIN TERC, CHLOROPLASTIC; 1.
DR   Pfam; PF03741; TerC; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        14..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        47..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        270..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        294..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   325 AA;  36510 MW;  AB86409F4BF465BB CRC64;
     MDAVSTTLSI GEPWMWGAFV GFVLAMLAVD LFLAGGNKAH KVGFKEAAAW SFVWFTLAML
     FNLGLWWYLK GSYGSEVADV KAMEFLTGYL IEKSLAVDNI FVFLMIFSFF AVPAEFQRRV
     LIYGVIGAIV MRAAMILAGA WLVKEFHWIL YLFGAFLAIT GIKMLMFAEA EPDLAKNPLL
     KWVKRHVRMT PDFRGEKFWV VENGVRVFTP LFLVLIMIEI SDLIFAVDSI PAIFAITTDP
     FIVFTSNIFA ILGLRAMYFM LAGMADRFHL LKYGLAIVLL FVGTKMLIVD FYKIPVGLSL
     GIVGFIIAGF MFASLWTTRK RAAPD
//
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