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Database: UniProt
Entry: M5CXT3_STEMA
LinkDB: M5CXT3_STEMA
Original site: M5CXT3_STEMA 
ID   M5CXT3_STEMA            Unreviewed;       637 AA.
AC   M5CXT3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   08-NOV-2023, entry version 25.
DE   SubName: Full=Putative polysaccharide biosynthesis protein epsC {ECO:0000313|EMBL:CCP10928.1};
GN   Name=wbiI {ECO:0000313|EMBL:CCP10928.1};
GN   ORFNames=SMSKK35_2327 {ECO:0000313|EMBL:CCP10928.1};
OS   Stenotrophomonas maltophilia SKK35.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=1118156 {ECO:0000313|EMBL:CCP10928.1, ECO:0000313|Proteomes:UP000012178};
RN   [1] {ECO:0000313|EMBL:CCP10928.1, ECO:0000313|Proteomes:UP000012178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKK35 {ECO:0000313|EMBL:CCP10928.1,
RC   ECO:0000313|Proteomes:UP000012178};
RA   Linke B., Adamek M., Schwartz T.;
RT   "Stenotrophomonas maltophilia SKK35 and RA8 genome sequencing: analysis and
RT   comparison of viurlence genes.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC       {ECO:0000256|ARBA:ARBA00007430}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCP10928.1}.
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DR   EMBL; CALN01000526; CCP10928.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5CXT3; -.
DR   Proteomes; UP000012178; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
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        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        109..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          288..570
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   637 AA;  70353 MW;  559E9838BDC2D488 CRC64;
     MASPWRDRIL GLMPRSAIVC HDLFMVWACW QLLHAGRYSI LPNAPELPLW NIDTTLVLLL
     QGLVFWRVGL YRGLWRFASV SDLLNIFKAS FIGMVAIVLV LMWKRFDGVP MSVLVIYPFA
     LSALLGAPRL LYRAWKDYQA LQSDSSARRV LILGAGQAAE TLVRDLRRSG NFEPVGLLDD
     APHLRGAKLQ GLPILGTLDD APTVVRETAA KLLVIAIPSL DAAGMQRIVA ICESTGVPFR
     TVPKLSDILQ GQSLPGQLKE VAIEDLLGRK PIMPDWNLIR GWLGGRTVMV TGAGGSIGSE
     LCRQCARHGA GRIILLEISE LLLLTIEGEL RRSFPDVEIE AVLGDCGDPA VIRHALSLHP
     VDTAFHAAAY KHVPVLERQL REAVRNNILA TENVARACLE ARVEHFVFIS TDKAVDPVNA
     LGASKRYAEM ICQSLDQKST HTRFVTVRFG NVLASAGSVV PLFREQILRG GPVTVTDPEV
     SRYFMTIPEA CQLILQAAAS ASHGAIYTLD MGEPVPIRLL AEQMIRLAGK QPYKDIPIIY
     TGLRPGEKLH ETLFYSDEDY RSTAHPKILE AGVRMFSRDL VLANVPRLRD AVCSYDTDTI
     KEVLFATMPE FSPIEQDAYI SSAKVVPFPA REANRHQ
//
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