ID A9M932_BRUC2 Unreviewed; 561 AA.
AC A9M932;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Capsular polysaccharide biosynthesis protein capD {ECO:0000313|EMBL:ABX61596.1};
GN Name=capD {ECO:0000313|EMBL:ABX61596.1};
GN OrderedLocusNames=BCAN_A0518 {ECO:0000313|EMBL:ABX61596.1};
OS Brucella canis (strain ATCC 23365 / NCTC 10854).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=483179 {ECO:0000313|EMBL:ABX61596.1, ECO:0000313|Proteomes:UP000001385};
RN [1] {ECO:0000313|EMBL:ABX61596.1, ECO:0000313|Proteomes:UP000001385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23365 / NCTC 10854 {ECO:0000313|Proteomes:UP000001385};
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL Submitted (OCT-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; CP000872; ABX61596.1; -; Genomic_DNA.
DR AlphaFoldDB; A9M932; -.
DR KEGG; bcs:BCAN_A0518; -.
DR HOGENOM; CLU_013560_6_0_5; -.
DR Proteomes; UP000001385; Chromosome I.
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 36..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 307..551
FT /note="Polysaccharide biosynthesis protein CapD-like"
FT /evidence="ECO:0000259|Pfam:PF02719"
SQ SEQUENCE 561 AA; 62065 MW; E2978C6C5593E521 CRC64;
MPGLVSLHLE GGITARMSLK YPWKRLALLP RISKQIILVL SDCLLLLASA YLAFVVRFGF
VFVPNLAQLF LILIAPLLAI PVFIRFGLYR AIIRYLAERA IWSIFQATAV AALFWVALVF
LMELYGSTGL PRSVPLLYWL LSTVFISASR FGAKWLLRTA EHDKRYTSSA LIIGIGEPAR
QLATALRSHS DTLVVGFIDP AGQLAGMDII GLRVYRTEEI PSLIENYGIK QVVVSEPALE
QKERQEFARL LGRLPVNTRI LPPIADLTAG KYLVSALRNV EIDDLLGRSP VPPDTTLLRE
VVEGRRIMIT GAGGSIGSQL CLTIAQWNPA AIVLFESSEF ALYQIDRQLR QFASCTVVPV
LGSVRDRACV EKTIRDHSID TVYHCAAYKH VPLVERNPLV GIFNNVFGTL EVAEAALNTD
VERMVLISSD KAVRPTNVMG ATKRWAELVV YYYGRLAEQA GKKKAFYSVR FGNVLGSNGS
VVPLFREQIA NGGPVTLTHE DMTRYFMSIK EAAELIVQSG AIAQSGDTVL LEMGEPVKIR
DLAENMIQRQ QGHHAGDQDC I
//
