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Database: UniProt
Entry: B1BNK0_CLOPF
LinkDB: B1BNK0_CLOPF
Original site: B1BNK0_CLOPF 
ID   B1BNK0_CLOPF            Unreviewed;       637 AA.
AC   B1BNK0;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Capsular polysaccharide biosynthesis protein {ECO:0000313|EMBL:EDT16725.1};
GN   ORFNames=AC3_0579 {ECO:0000313|EMBL:EDT16725.1};
OS   Clostridium perfringens E str. JGS1987.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=451755 {ECO:0000313|EMBL:EDT16725.1, ECO:0000313|Proteomes:UP000005337};
RN   [1] {ECO:0000313|EMBL:EDT16725.1, ECO:0000313|Proteomes:UP000005337}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E str. JGS1987 {ECO:0000313|Proteomes:UP000005337};
RA   Paulsen I., Sebastian Y.;
RT   "Annotation of Clostridium perfringens E str. JGS1987.";
RL   Submitted (JUL-2007) 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:EDT16725.1}.
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DR   EMBL; ABDW01000001; EDT16725.1; -; Genomic_DNA.
DR   RefSeq; WP_003461211.1; NZ_ABDW01000001.1.
DR   AlphaFoldDB; B1BNK0; -.
DR   Proteomes; UP000005337; 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   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; 2.
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        9..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        44..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        77..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        109..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          292..575
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   637 AA;  71451 MW;  3DE70C522775D36C CRC64;
     MEKEGKVKAL FLMSLDTLII VNSYILAFII RFNFDFIMDE RNGLILFLPV IVTIYLMMLS
     IFKMYKSIWT IVGIDEVAFG LIACLIATGI ILITSTIISS IYYIDHITVL LAGLFIMIFT
     IGIRVSFRIY RRMISHGRVL LNSSNISNLE KILIIGAGSC GQLIIEEIRK QNPIKQKVIG
     VIDDNPSKIG TYLRGIKILG NRNKIIEISE EKNVDLILIA MPSVDGKTKK EIIEICQSTR
     AKVKIIPGMY ELIGGKVSLN RMRDIDLRDL LGREEVILDK KGIKDYIENK VVMVTGGGGS
     IGSELCRQIA KFSPKLLLIL DIYENNAYEL ENEIISNFKN LKEKVLIASV REEKRLENIF
     NEYKPQVIFH AAAHKHVPLM ERNPEEAIKN NVIGTLNVAE CAHKYGAERF VLISTDKAVN
     PTNVMGASKR MCEMIIQAID KNSNTEFVAV RFGNVLGSNG SVIPLFKKQI AKGGPVTLTH
     KKITRYFMLI PEAAQLVLQA GAYAKGGEIF VLDMGNPVLI YDLAKDLIKL SGFEPEVDIK
     IEITGLRPGE KLYEELLMDE EGLRKTSHEK IFIAKPGEYD FEMLKLGVNA LKKIADLGDV
     ETLKTALQFI VKTYKRLDTE NNSVFNEVAL HEASEAI
//
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