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Database: UniProt
Entry: A1BJP2_CHLPD
LinkDB: A1BJP2_CHLPD
Original site: A1BJP2_CHLPD 
ID   A1BJP2_CHLPD            Unreviewed;       682 AA.
AC   A1BJP2;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Polysaccharide biosynthesis protein CapD {ECO:0000313|EMBL:ABL66619.1};
GN   OrderedLocusNames=Cpha266_2635 {ECO:0000313|EMBL:ABL66619.1};
OS   Chlorobium phaeobacteroides (strain DSM 266 / SMG 266 / 2430).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290317 {ECO:0000313|EMBL:ABL66619.1, ECO:0000313|Proteomes:UP000008701};
RN   [1] {ECO:0000313|EMBL:ABL66619.1, ECO:0000313|Proteomes:UP000008701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 266 {ECO:0000313|EMBL:ABL66619.1,
RC   ECO:0000313|Proteomes:UP000008701};
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., Pitluck S., Goltsman E.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL   Submitted (DEC-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; CP000492; ABL66619.1; -; Genomic_DNA.
DR   RefSeq; WP_015961150.1; NC_008639.1.
DR   AlphaFoldDB; A1BJP2; -.
DR   STRING; 290317.Cpha266_2635; -.
DR   KEGG; cph:Cpha266_2635; -.
DR   eggNOG; COG1086; Bacteria.
DR   HOGENOM; CLU_013560_5_0_10; -.
DR   Proteomes; UP000008701; 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   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008701};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        84..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          293..586
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
FT   REGION          654..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   682 AA;  75582 MW;  9AAD716FF299DC1A CRC64;
     MKRYIFLFGK YILDSPRYVK WLIAVGFDLF SALITVWLAC SLRLESISLP DLTHLRLYLL
     APALMLPIFT LFGLYHAIHR YSGFSVFITV GKAMLVYGFA FFSIMLLMQI DGIPRSIGIL
     QPILLFLMTA GSRAMVRFMY TAATSHSMRG RSLDRLLIYG AGSSGAEIGK ALQERANYEL
     LGYLDDSKEL HGRKLNGIPV YYPGEAERLI QKEGINNVLI AMPSASRTRR NEIIESFRRY
     PVRIQTLPGV DELADGRVTI SDIKEVEIED LLGRDPVPID HELVHRAITK KVVLVTGAGG
     SIGSELCRQL LQAHPATLLL LDNTELNLYT IHCDVEARAQ KIQAATRFVP LLCDVTDEER
     ITEICRVFKP EVIYHAAAYK HVPMVEYNPA EGVRNNVFGT LSVVRAAIRQ GVSNFVLVST
     DKAVRPTNVM GASKRLCEMA LQAHAAEQGH KTCFSMVRFG NVLGSSGSVV PLFRRQIKEG
     NAITITHEEI TRYFMTIPEA AQLIIQAGAM ATGGDLYLLE MGKPVKIIDL ARKMVELSGL
     SVRDHENPNG DIEIKVTGLR PGEKLYEELL IGNNSGPTAN PRIFKAYEEF MPIGELNTEL
     SQLIVAIRVN DVKNIKRILN KIIPEYNPAA ETTDLLASET ECQICANISR PKKVQSNGKN
     GKTVKSAELG VMGNGKSGSR TC
//
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