ID A0A1E4NEW4_9PROT Unreviewed; 489 AA.
AC A0A1E4NEW4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Lipopolysaccharide biosynthesis protein {ECO:0000313|EMBL:ODU90529.1};
GN ORFNames=ABT21_00285 {ECO:0000313|EMBL:ODU90529.1};
OS Thiobacillus sp. SCN 65-179.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1660144 {ECO:0000313|EMBL:ODU90529.1, ECO:0000313|Proteomes:UP000094681};
RN [1] {ECO:0000313|EMBL:ODU90529.1, ECO:0000313|Proteomes:UP000094681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC {ECO:0000256|ARBA:ARBA00007430}.
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:ODU90529.1}.
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DR EMBL; MEGN01000001; ODU90529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4NEW4; -.
DR STRING; 1660144.ABT21_00285; -.
DR Proteomes; UP000094681; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR CDD; cd13127; MATE_tuaB_like; 1.
DR InterPro; IPR029303; Polysacc_synt_C.
DR PANTHER; PTHR30250:SF10; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN WZXC-RELATED; 1.
DR PANTHER; PTHR30250; PST FAMILY PREDICTED COLANIC ACID TRANSPORTER; 1.
DR Pfam; PF13440; Polysacc_synt_3; 1.
DR Pfam; PF14667; Polysacc_synt_C; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 443..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 325..464
FT /note="Polysaccharide biosynthesis protein C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14667"
SQ SEQUENCE 489 AA; 53261 MW; BFAAADF2A5E66078 CRC64;
MSLGDSIRHG AKWVFIGNTG SQVLNFALGL ILARLLMPAE FGMVATILIF TNLAGFVAGG
GMGQAIVRAK EATKRDFDLL FTLQSLIGLV IVGFFFVIAP AFGRWYGDPL YTDMLRIAAL
SFLIRPFFNV PSNMLHRDMR FKAKTAVQLT NLFVYNGIAL SLAWKGYGPW SLILASIFSS
VAGAAQFAWY ARWRPGLCFD FARAGELMRY GLLASSNNIV GYVRNQLPTF ILSRSLGPAG
VGLYNKAESL AARPHGFITG SVYEVLFRAL AKEHDDLDKS RYLFFRSLTL VLVYALPFYV
GFAWVAEPLV VLLFGHRWAD SAAPLVILSL AAPFMIVENL SGAVLAARNW LGRELVAQIL
MIGIAGTGII LGLPHGMEGV AAGMAIALLY MSVHMFWLAR RCLQARWRDL GRAFVPALLL
NGILAATLWL VDASLPAALR ANGPLYVILM AAAGGLVYAL GFLYLPIPAL ASESARWKTK
LRLSPSTAA
//
