ID   A0A2T4UA21_9BACI        Unreviewed;       605 AA.
AC   A0A2T4UA21;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Polysaccharide biosynthesis protein CapD-like domain-containing protein {ECO:0000259|Pfam:PF02719};
GN   ORFNames=C6Y45_02285 {ECO:0000313|EMBL:PTL40229.1};
OS   Alkalicoccus saliphilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalicoccus.
OX   NCBI_TaxID=200989 {ECO:0000313|EMBL:PTL40229.1, ECO:0000313|Proteomes:UP000240509};
RN   [1] {ECO:0000313|EMBL:PTL40229.1, ECO:0000313|Proteomes:UP000240509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6AG {ECO:0000313|EMBL:PTL40229.1,
RC   ECO:0000313|Proteomes:UP000240509};
RA   Zhao B.;
RT   "Alkalicoccus saliphilus sp. nov., isolated from a mineral pool.";
RL   Submitted (MAR-2018) 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:PTL40229.1}.
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DR   EMBL; PZJJ01000002; PTL40229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4UA21; -.
DR   OrthoDB; 9803111at2; -.
DR   Proteomes; UP000240509; 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        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          278..558
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   605 AA;  68025 MW;  97D095A63715AB46 CRC64;
     MTYRKRFGMF TLLDTLIIIA AFSSSFIIVD VAGILFSMTF WISVFIILIS YYMSAFYFRM
     NRKAWEYASI GELKNIVKTL TAAVVLNGII QMAVFSYVLY RVLFVTWILM ILGIGGARFF
     RRYRNESTYR KKLGRKKTMI IGAGSAGMML ARQLSQSRGC ELDPVVFIDD DPYKQQLDIL
     SLPVAGNTEQ IPELAKIYEV ERIIIAIPSM ERKKLHDIYE ICLKTGIKTQ VLPMIEDLVT
     GKLSVTQLRD VSPEDLLGRE EVELDHKHIK TSMRGKTVMV TGAGGSIGSE LCRQIVKYKP
     ARLILLGHGE NSIYHIQMEL MKHKPETILT PLIADIQDRI RIHEVMEEWK PDQVYHAAAH
     KHVPLMEENP QEAVKNNTIG SLNVAEAADA AGVKTVVMVS TDKAVNPTSV MGASKRLAEM
     LIHHLNSRSS TIYTVVRFGN VLGSNGSVIP LFKKQIDQGG PVTVTHPEMV RYFMTIPEAS
     RLVLQAGTMA KGGETFVLDM GEPVKIVDLA KNLITLSGYT MDEIPIQFTG MRPGEKLYEE
     LLNEEEIHDE QIFPKIYLGR ASTLPLEEIE NLLSDFTALE KEQLRNIMLE LTNRRIVAVG
     ESTTA
//