ID Q01WZ5_SOLUE Unreviewed; 637 AA.
AC Q01WZ5;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Polysaccharide biosynthesis protein CapD {ECO:0000313|EMBL:ABJ85820.1};
GN OrderedLocusNames=Acid_4861 {ECO:0000313|EMBL:ABJ85820.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ85820.1};
RN [1] {ECO:0000313|EMBL:ABJ85820.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ85820.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Janssen P.H., Kuske C.R., Richardson P.;
RT "Complete sequence of Solibacter usitatus Ellin6076.";
RL Submitted (OCT-2006) 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; CP000473; ABJ85820.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01WZ5; -.
DR STRING; 234267.Acid_4861; -.
DR KEGG; sus:Acid_4861; -.
DR eggNOG; COG1086; Bacteria.
DR HOGENOM; CLU_013560_5_0_0; -.
DR InParanoid; Q01WZ5; -.
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 14..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..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 289..573
FT /note="Polysaccharide biosynthesis protein CapD-like"
FT /evidence="ECO:0000259|Pfam:PF02719"
SQ SEQUENCE 637 AA; 70496 MW; D96B907CB4B3C5C0 CRC64;
MKNHRNIDVW LERACHLTVV GLSLTAAFLL RFDFAIPASV VPIWKQALLI AILVKLPIFD
WVGFYRSLRR FVSIPDLYLV FLGNVAGSLL LAAMSMFFTG PAMPRSVLIM DGILCFVATA
LVRFSVRIYN ATFRERSAEQ RTGILIYGAG AAGAELAREI HANRNTKYEV KGFLDDDPLK
QNARIMGIPV LGQGREAYSV VRQRNRRGPS VGEIIIAMPS ATGQQMRETL ANCRAAGVPC
KTIPGIDELL SGRVLLAQVR NPSVQDLLGR QQVRLDEAHV AASIAGRSVL VTGAAGSIGS
ELCRQVARFG PGCLIAFDQA ESDLFRIENE LRERYPELEL VTALGNIREA ERLSEVMRQH
AVESIFHAAA YKHVPMMESH PLEAVCNNVL GTWNLVRAAR GHNVRNLLMI SSDKAVNPSC
VMGATKRVCE RIVSSRWPGN GQTKCVSVRF GNVLGSNGSV VPVFQAQIAA GGPIKVTHPD
ARRFFMTISE AVSLVIQAST RTEGSEIFVL DMGEPIRIVD LAENMIRLAG KVPYEDIDIQ
FTGMRPGEKL MEEIRGKSER LIPTSMEKMH AIQEQPLVWD KINGWIEELK ELIAERQERR
IIAHLQTLVP EYTPSMRGAP QPVIMLPVKR PSELRSA
//