ID A8AWX7_STRGC Unreviewed; 350 AA.
AC A8AWX7;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Membrane protein, putative {ECO:0000313|EMBL:ABV09672.1};
GN OrderedLocusNames=SGO_0998 {ECO:0000313|EMBL:ABV09672.1};
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705 {ECO:0000313|EMBL:ABV09672.1, ECO:0000313|Proteomes:UP000001131};
RN [1] {ECO:0000313|EMBL:ABV09672.1, ECO:0000313|Proteomes:UP000001131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288
RC {ECO:0000313|Proteomes:UP000001131};
RX PubMed=17720781; DOI=10.1128/JB.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(2007).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000725; ABV09672.1; -; Genomic_DNA.
DR RefSeq; WP_012000415.1; NC_009785.1.
DR AlphaFoldDB; A8AWX7; -.
DR STRING; 467705.SGO_0998; -.
DR KEGG; sgo:SGO_0998; -.
DR eggNOG; COG1835; Bacteria.
DR HOGENOM; CLU_055093_0_0_9; -.
DR Proteomes; UP000001131; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF2; O-ACETYLTRANSFERASE WECH; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001131};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..325
FT /note="Acyltransferase 3"
FT /evidence="ECO:0000259|Pfam:PF01757"
SQ SEQUENCE 350 AA; 41398 MW; 1ED641DB22FAAAE3 CRC64;
MVEKEVKEQE RSVNYAMLSL FQYVASILVI LVHCQRLFPN EILHFTQKSM FGRMAVPFFL
ISSAFMLKSS LAKKKSMRTY VSRVLKQYIF WSILYLPYAL IYFWSLPVEK YYAPLALIAG
FLYIGLCYQL WYIPAFLLGL WIVHYLYKKV GPKWAIVVSL VLYLLGSIET YYTYFANTWP
THLYDVYSRI FFSTRNGLFY APIFILFGYL LYDYWNSNFF KKYIGKKFLL ASILLALDGW
LVFVNQGIDK NFFLALLPFS LFLVNGVLRT EIGKKWELYH LKKLSVLYFF LHPIFIESSF
YLLRETNISN WHKGQIVFVL TIALTHLTSE IILKFRKSVF ARQKNGNKTV
//
