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
//