ID   A0A0F2S8H1_9FIRM        Unreviewed;       614 AA.
AC   A0A0F2S8H1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Polysaccharide biosynthesis protein {ECO:0000313|EMBL:KJS46521.1};
GN   ORFNames=VR66_25085 {ECO:0000313|EMBL:KJS46521.1};
OS   Peptococcaceae bacterium BRH_c23.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629714 {ECO:0000313|EMBL:KJS46521.1, ECO:0000313|Proteomes:UP000033503};
RN   [1] {ECO:0000313|EMBL:KJS46521.1, ECO:0000313|Proteomes:UP000033503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c23 {ECO:0000313|EMBL:KJS46521.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KJS46521.1}.
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DR   EMBL; LADV01000315; KJS46521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2S8H1; -.
DR   PATRIC; fig|1629714.3.peg.541; -.
DR   Proteomes; UP000033503; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd05237; UDP_invert_4-6DH_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003869; Polysac_CapD-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43318:SF1; POLYSACCHARIDE BIOSYNTHESIS PROTEIN EPSC-RELATED; 1.
DR   PANTHER; PTHR43318; UDP-N-ACETYLGLUCOSAMINE 4,6-DEHYDRATASE; 1.
DR   Pfam; PF13727; CoA_binding_3; 1.
DR   Pfam; PF02719; Polysacc_synt_2; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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        32..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          281..564
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   614 AA;  67894 MW;  27940307E6C61932 CRC64;
     MLIDAMLINL AAFGSFYLRF EEGIPLDYYQ TYYHTAIGAT ILYLAVFYVF GLYNRLWQYA
     STGELLSIVY AVTVGTGGTV AVVYFYGLSN AATLSYVRMP HTAAMLLWLA MVFLIGGSRF
     IWRILQENAF ERHVPGSQKQ VLIVGAGDAG VLAARELKNR NYRDGRPVAF IDDDHSKQKL
     QLLGIPVLGT RKDIARIVKG HNVDEVIIAM PSASGESVRE IVQICEKLGV ELKIMPGVYD
     IISGDINVNP IRQVQVEDLL GRDPVSVDLE EVAGYVSGET VFITGAGGSI GSEICRQIAR
     FNPGKLVLLG HGENSIFDIE QELRAERPGI DYITEILDIK DREKVFLIFN RYKPGVVFHA
     AAHKHVPLME RNPEEAMKNN VIGTQNLAEA ADKINVKTFV SISTDKAVNP TSVMGATKRT
     AEMIIQSLDL RSNTKFVAVR FGNVLGSRGS VIPTFKRQIA QGGPVTVTHP DMVRYFMTIP
     EAAQLVIQAG AMALGGEIFI LDMGKPVKIV DLAKDLIRLS GFEPDVDIKI QFTGIRPGEK
     LFEELLTAEE GVTSTKHSRI FVAKPNHINV ELLEELTHKV RDRGSYLTRD EVIELLQTVI
     PAFRKKATKT AVNQ
//