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Database: UniProt
Entry: A5V0V8_ROSS1
LinkDB: A5V0V8_ROSS1
Original site: A5V0V8_ROSS1 
ID   A5V0V8_ROSS1            Unreviewed;       648 AA.
AC   A5V0V8;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   SubName: Full=Polysaccharide biosynthesis protein CapD {ECO:0000313|EMBL:ABQ92511.1};
GN   OrderedLocusNames=RoseRS_4167 {ECO:0000313|EMBL:ABQ92511.1};
OS   Roseiflexus sp. (strain RS-1).
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ92511.1, ECO:0000313|Proteomes:UP000006554};
RN   [1] {ECO:0000313|Proteomes:UP000006554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554};
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   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT   "Complete sequence of Roseiflexus sp. RS-1.";
RL   Submitted (APR-2007) 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; CP000686; ABQ92511.1; -; Genomic_DNA.
DR   RefSeq; WP_011958848.1; NC_009523.1.
DR   AlphaFoldDB; A5V0V8; -.
DR   STRING; 357808.RoseRS_4167; -.
DR   KEGG; rrs:RoseRS_4167; -.
DR   eggNOG; COG1086; Bacteria.
DR   HOGENOM; CLU_013560_5_0_0; -.
DR   OMA; KHNTQIN; -.
DR   OrthoDB; 9803111at2; -.
DR   Proteomes; UP000006554; 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   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   SMART; SM00822; PKS_KR; 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        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        36..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          288..575
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   648 AA;  71148 MW;  BE49F62AA1ED2F57 CRC64;
     MMQRLQNRHF LLFDILLVPL AIYLSFVLRL EMFNLGSYWL VCMQFCLTAV VTTPLVFRAL
     GIYRRYWRYA SFEELLLLCS ATSIALALAT LVFTLIDALL PVVATMPRSI PFIVPPIAAT
     LISVPRLLVR IGAARERRRR ATDRPAPVLI MGAGDAASII VREIQRNPKL GMEVVGLLDD
     DPAKRGLRLH GVEVMGDRHA IPTLVARHKV RQVIIAMPGA PGKAVREIMH ICESVGVTVR
     IMPGVHELID GTISVSKLRN IQIEDLLRRA PVQTDTAAVR ALIANRRVLV TGGGGSIGSE
     LCRQLIRCGP SHLIVLGHGE NSVFEICNEL QRLAEAHAGQ SPHIVPVIAD IRDLERLRAV
     FEMHAPELVF HAAAHKHVPL MEEHPVEAIS NNVIGTRNLL DVSLETGVER FVMISSDKAV
     NPTSVMGATK RIAEMLVLNA ARISGRPYVA VRFGNVLGSR GSVVLTFKRQ IAAGGPVTVT
     HPEMRRYFMT IPEAVQLVLQ ASVLGRAGEI FMLDMGEPVK VVDLARDMIR LSGLEVGRDI
     DICFTGIRPG EKLFEELFAH GEEYQPTAHS KIFIAAGASN NIPPDLRTDV ALLEQVARAN
     DDAAARRMLR HIVPEYCPPL PAPPIPVAEN TPYPVLVRPL QPLIGGGR
//
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