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Database: UniProt
Entry: A0A0G1S4G0_9BACT
LinkDB: A0A0G1S4G0_9BACT
Original site: A0A0G1S4G0_9BACT 
ID   A0A0G1S4G0_9BACT        Unreviewed;       345 AA.
AC   A0A0G1S4G0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Conserved membrane protein {ECO:0000313|EMBL:KKU64282.1};
GN   ORFNames=UX86_C0010G0012 {ECO:0000313|EMBL:KKU64282.1};
OS   Candidatus Amesbacteria bacterium GW2011_GWC1_47_15.
OC   Bacteria; Candidatus Amesbacteria.
OX   NCBI_TaxID=1618364 {ECO:0000313|EMBL:KKU64282.1, ECO:0000313|Proteomes:UP000034502};
RN   [1] {ECO:0000313|EMBL:KKU64282.1, ECO:0000313|Proteomes:UP000034502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the acyltransferase 3 family.
CC       {ECO:0000256|ARBA:ARBA00007400}.
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:KKU64282.1}.
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DR   EMBL; LCNU01000010; KKU64282.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1S4G0; -.
DR   STRING; 1618364.UX86_C0010G0012; -.
DR   Proteomes; UP000034502; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   InterPro; IPR002656; Acyl_transf_3_dom.
DR   PANTHER; PTHR40074; O-ACETYLTRANSFERASE WECH; 1.
DR   PANTHER; PTHR40074:SF3; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE EXPORT PROTEIN-RELATED; 1.
DR   Pfam; PF01757; Acyl_transf_3; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        51..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        95..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        158..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        253..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        283..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        317..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..334
FT                   /note="Acyltransferase 3"
FT                   /evidence="ECO:0000259|Pfam:PF01757"
SQ   SEQUENCE   345 AA;  39589 MW;  9533A4BE9CFD19CE CRC64;
     MWYNSAVRAT KKNHNGAIDA IRIAAILGVI MIHTTTRILE TSRFDVQNYQ LTLFLNQAAR
     FAVPVFFMIS GYVLQLSYKP SAGYFEYLKK RLNRIFVPYV LWSAIYYLFV YKQHNFSFPT
     ALMTGAASYQ LYFLPALLVC YLIFPVLYKY FKKLTENTTL SGLGAAQFGL LYYNYFVKPL
     PIFYPAGVAL LNIFVFILGM GAAGNEDRLQ EAVRRNKNIL MICVLFLAGY IFIEGKSRYL
     QSGNYLAFYS SWRPSVLVYS IIAAWLMYYF FQKHQIFASL IKTMSGLSFL VFFIHVAVLE
     TVWSGAGDLI FRYMPNFGFF ALTAGFSYFT AFALHKIKPL AKFTG
//
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