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Database: UniProt
Entry: A0A117SEM5_9FLAO
LinkDB: A0A117SEM5_9FLAO
Original site: A0A117SEM5_9FLAO 
ID   A0A117SEM5_9FLAO        Unreviewed;       639 AA.
AC   A0A117SEM5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Polysaccharide biosynthesis protein {ECO:0000313|EMBL:KUO67263.1};
GN   ORFNames=APF83_11760 {ECO:0000313|EMBL:KUO67263.1};
OS   Lutibacter sp. BRH_c52.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lutibacter.
OX   NCBI_TaxID=1734397 {ECO:0000313|EMBL:KUO67263.1, ECO:0000313|Proteomes:UP000054346};
RN   [1] {ECO:0000313|EMBL:KUO67263.1, ECO:0000313|Proteomes:UP000054346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c52 {ECO:0000313|EMBL:KUO67263.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) 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:KUO67263.1}.
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DR   EMBL; LOEY01000043; KUO67263.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117SEM5; -.
DR   Proteomes; UP000054346; Unassembled WGS sequence.
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        9..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          296..578
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   639 AA;  72941 MW;  2A948AE621FF4240 CRC64;
     MLRKIRKQFF IRSAPSWLVL AIDLYWVINN FLFAHLIRFN FKFSLDGSVL KIQLPVVIAI
     TVFSFLITGS YRGIIRHTGS KDAIKVITAS FLIMVFLMVT VFLVNYLNWD EILDFPFSII
     VIHFLLNTLV LIGLRFLFKI FYDILFSSYK VGPKILIYGA GEAGLLTYSI FNNDKANNSQ
     ICGFIDDDPR KHNKRINGVR VYNPKDVTQE FITDKKITRI IIAMQFIKQA RLIEIVAQLT
     KLSVKVKIVP PTRTWINRPG LKVAQIKSIN IEDLLGRSVI EMDNPELEKE FNNKVVLITG
     AAGSIGSEIC RQLSNFNYKH LILVDQAESD LYNLQQYFNY KKYLNITCIV ADVRNEKRMD
     SIFEKFKPNM VFHAAAYKHV PFMEENPYEA VLVNVFGTKT IADLVIKHQA KKFVMVSTDK
     AVNPTNVMGA TKRIAEMYIT SLQGKGASKF ITTRFGNVLG SSGSVIPLFK TQIKNGGPIT
     LTHKDITRYF MTIPEACQLV LEAGIMGDGG EIFVFDMGTP IKIYDLALNM IQLSNLKYPE
     DINIEITGLR PGEKIYEELL GDGENCIPTH HHKIMIAKVK TMDVNEIQQK INELCVCNRE
     LNFEQTVSKM KEIVPEFISN NSVYEKFDHI EQLKIKTEE
//
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