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Database: UniProt
Entry: B9E5U1_CLOK1
LinkDB: B9E5U1_CLOK1
Original site: B9E5U1_CLOK1 
ID   B9E5U1_CLOK1            Unreviewed;       612 AA.
AC   B9E5U1;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Polysaccharide biosynthesis protein CapD-like domain-containing protein {ECO:0000259|Pfam:PF02719};
GN   OrderedLocusNames=CKR_2815 {ECO:0000313|EMBL:BAH07866.1};
OS   Clostridium kluyveri (strain NBRC 12016).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=583346 {ECO:0000313|EMBL:BAH07866.1, ECO:0000313|Proteomes:UP000007969};
RN   [1] {ECO:0000313|Proteomes:UP000007969}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12016 {ECO:0000313|Proteomes:UP000007969};
RA   Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA   Yukawa H.;
RT   "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT   of Clostridia species.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC       {ECO:0000256|ARBA:ARBA00007430}.
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DR   EMBL; AP009049; BAH07866.1; -; Genomic_DNA.
DR   RefSeq; WP_012103520.1; NC_011837.1.
DR   AlphaFoldDB; B9E5U1; -.
DR   KEGG; ckr:CKR_2815; -.
DR   HOGENOM; CLU_013560_5_2_9; -.
DR   Proteomes; UP000007969; Chromosome.
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..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        72..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          287..569
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   612 AA;  70038 MW;  31ABE0B81A02B47B CRC64;
     MQKDKKLIVY DIFFLIASLY FALLLRFEFN VPSEYMIFFK LSVVPVVIVT LICNKFFNLY
     NNIWKYASVE ELISIVYSVS LSNIIFIIYS YFVNYKILEN RYYRFPYTVH IILWILSVLA
     LGGIRFTYRL SGDKKEENCT KRRHKNLLII GAGDAAAMLI KEIKKHTNFN YNIIGLIDDD
     KSKRGKLIKG IEVLGGRNEI IEVCKNRQIE EIIIAMPSAE LHTKREIINI CKNTKCKLKT
     LPGIYEMIDG NINITKLRDV NIEDLLGREE VKLNTQNISK YIKNKIIMVT GGGGSIGSEL
     CRQIAKFQPK QLLILDIYEN NVYDLEMELN YNYIDLNKKI IIASIRDGGR LKDVFRKYTP
     QVVFHAAAHK HVPLMEGNPQ EAVKNNIIGT YEVLKCCDEF KVEKFVQIST DKAVNPTNVM
     GATKRFCEIM VQAFNEVSKT EYVAVRFGNV LGSNGSVIPL FKRQIAHGGP VTVTHPEINR
     FFMTIPEAAQ LVIQAGAIAA GGEIFVLDMG KPVKIVDLAR DLITLSGYEP DMDIKIEYTG
     LRPGEKLYEE LLMNEVALTS TEHDKIFIEK PAKIDMNFIE KSIGEFKEVL DQDKEQIIQL
     IEKKVPTYKR KK
//
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