ID S9QRP7_9RHOB Unreviewed; 676 AA.
AC S9QRP7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acyltransferase 3 {ECO:0000313|EMBL:EPX82318.1};
GN ORFNames=Salmuc_04043 {ECO:0000313|EMBL:EPX82318.1};
OS Salipiger mucosus DSM 16094.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX82318.1, ECO:0000313|Proteomes:UP000015347};
RN [1] {ECO:0000313|Proteomes:UP000015347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX PubMed=25197501; DOI=10.4056/sigs.4909790;
RA Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT clade.";
RL Stand. Genomic Sci. 9:1331-1343(2014).
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:EPX82318.1}.
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DR EMBL; APVH01000023; EPX82318.1; -; Genomic_DNA.
DR RefSeq; WP_020040556.1; NZ_KE557275.1.
DR AlphaFoldDB; S9QRP7; -.
DR STRING; 1123237.Salmuc_04043; -.
DR eggNOG; COG1835; Bacteria.
DR HOGENOM; CLU_005679_10_2_5; -.
DR OrthoDB; 9796461at2; -.
DR Proteomes; UP000015347; Unassembled WGS sequence.
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 InterPro; IPR043968; SGNH.
DR PANTHER; PTHR23028:SF136; ACETYLATION OF THE O-ANTIGEN (LPS); 1.
DR PANTHER; PTHR23028; ACETYLTRANSFERASE; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
DR Pfam; PF19040; SGNH; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:EPX82318.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000015347};
KW Transferase {ECO:0000313|EMBL:EPX82318.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..334
FT /note="Acyltransferase 3"
FT /evidence="ECO:0000259|Pfam:PF01757"
FT DOMAIN 399..666
FT /note="SGNH"
FT /evidence="ECO:0000259|Pfam:PF19040"
SQ SEQUENCE 676 AA; 73996 MW; 1D9EC8D97536CE2D CRC64;
MPTPENRSLP YRSEIDGLRA IAVIAVVLYH FGVPGLSGGF VGVDVFFVIS GFLIGGILWR
EYDATGRIWL RHFYMRRFRR LAPAFFTMAA VTTLLAWALL LPFEFREYGK ALISATVYLS
NVLFYRQAGY FDTASEDKPL LHTWSLAVEE QFYIFLPLFI LLLSRNRRAL LLALAGCWAA
SLAACIWLTP THPSATFYLF PFRAWELLSG VLLAIWGIET GRRWRGYAVL SWLGLALVLA
SVLLIPAGRH FPGLLAMAPV LGTVLLLANG TGMNPVNRLL SAPGPVFFGR ISYSLYLWHW
PVLTLSLYLR GGYSSWAETL AWMAVSVVLA WLSWRLVEAP MRRARLPGFV FLGGTVAASA
AMLAVGGWLY VKDGLPGRFG AEVRPHIAAS GDFLQDWSRC HRPTEGPLMG LEVCPIGPEG
APRVLVWGDS HVRAVKEGLD RTAHEAGTPG LILWRAGCPP LFGLRKTESA ATPAQDTACT
QANLQIRQAL PRLDSLDKVL LVGRWAYYAT GTGVGLDEAN RIAIHPAEAP RQVGVPQVET
LTEAAETTVS GLLDHFDEVI VLRQPPEVAQ YDSRLAAREA AHAGWPLARA PVTETAIPRT
ALSARADAAD APWQDMAEAG AISWIDPWPR LCDDAACHAL VEGTGYYFDN NHLTNSAALA
LRGLFARVFT PEGAGS
//
