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Database: UniProt
Entry: A0A1B6B8M2_9FIRM
LinkDB: A0A1B6B8M2_9FIRM
Original site: A0A1B6B8M2_9FIRM 
ID   A0A1B6B8M2_9FIRM        Unreviewed;       332 AA.
AC   A0A1B6B8M2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=GDT1 family protein {ECO:0000256|RuleBase:RU365102};
GN   ORFNames=F3D3_0676 {ECO:0000313|EMBL:GAU76079.1};
OS   Fusibacter sp. 3D3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XII. Incertae Sedis; Fusibacter.
OX   NCBI_TaxID=1048380 {ECO:0000313|EMBL:GAU76079.1, ECO:0000313|Proteomes:UP000095197};
RN   [1] {ECO:0000313|EMBL:GAU76079.1, ECO:0000313|Proteomes:UP000095197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D3 {ECO:0000313|EMBL:GAU76079.1,
RC   ECO:0000313|Proteomes:UP000095197};
RA   Serrano A.E., Escudero L.V., Encalada O., Tebes C.J., Fernandez S.,
RA   Demergasso C.S.;
RT   "Draft genome sequence of Fusibacter ascotence 3D3 isolated from the high
RT   arsenic level Ascotan salt flat in northern Chile.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU365102}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU365102}.
CC   -!- SIMILARITY: Belongs to the GDT1 family. {ECO:0000256|ARBA:ARBA00009190,
CC       ECO:0000256|RuleBase:RU365102}.
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:GAU76079.1}.
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DR   EMBL; BDHH01000002; GAU76079.1; -; Genomic_DNA.
DR   RefSeq; WP_069871173.1; NZ_BDHH01000002.1.
DR   AlphaFoldDB; A0A1B6B8M2; -.
DR   STRING; 1048380.F3D3_0676; -.
DR   OrthoDB; 9801356at2; -.
DR   Proteomes; UP000095197; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001727; Gdt1.
DR   PANTHER; PTHR12608:SF1; TRANSMEMBRANE PROTEIN 165; 1.
DR   PANTHER; PTHR12608; TRANSMEMBRANE PROTEIN HTP-1 RELATED; 1.
DR   Pfam; PF01169; UPF0016; 2.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365102};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095197};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU365102};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU365102}.
FT   TRANSMEM        36..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365102"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365102"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365102"
FT   TRANSMEM        164..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365102"
FT   TRANSMEM        194..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365102"
SQ   SEQUENCE   332 AA;  37186 MW;  D997950A0D904748 CRC64;
     MSDFLRALLL IFIAEMGDKT QIMAMAFATK YKVNHILLGV AIGSFANHGI AILLGSLLNR
     FIPIEALQLV AGVLFISFGL LSLSIAEEEE AEQNLKKYGA IVTVGIAFFL GELGDKTQLT
     AMTLATDSVN PAFTLMGTVL GMVVVSSVGI FVGAKLGNRI PEHLIKFGAF LIFMFFGLNK
     IFTSPYVQSM GMTFMALLVF MISILTIFRF MIFNRQLKEV SISALKQKAQ DLKTYRERIL
     ENLNGLCKQC DVCKEHQCLV GYMKDLLSQK VDIKAIDHAF IEALYDDHFD ACQAEQILTL
     LKEYFNKYPE EHLVNLELIN IEKVLNKIIK KE
//
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