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Database: UniProt
Entry: A0A1G7RZF3_9LACT
LinkDB: A0A1G7RZF3_9LACT
Original site: A0A1G7RZF3_9LACT 
ID   A0A1G7RZF3_9LACT        Unreviewed;       626 AA.
AC   A0A1G7RZF3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC {ECO:0000313|EMBL:SDG16163.1};
GN   ORFNames=SAMN05421791_103239 {ECO:0000313|EMBL:SDG16163.1};
OS   Facklamia miroungae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX   NCBI_TaxID=120956 {ECO:0000313|EMBL:SDG16163.1, ECO:0000313|Proteomes:UP000199708};
RN   [1] {ECO:0000313|EMBL:SDG16163.1, ECO:0000313|Proteomes:UP000199708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-466 {ECO:0000313|EMBL:SDG16163.1,
RC   ECO:0000313|Proteomes:UP000199708};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNCK01000003; SDG16163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7RZF3; -.
DR   STRING; 120956.SAMN05421791_103239; -.
DR   Proteomes; UP000199708; 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   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:UP000199708};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        57..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          300..581
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   626 AA;  70205 MW;  24F16FDA716CBCB3 CRC64;
     MLKRQEEVSR RFVQWVEKLP LIHKRLIWAM SDFVSFGIAT TISLIIFLGI LKVPVTFYLG
     HLVLSFLFYF FICKYLRVES RIKRYATMID IISLFLIVLF ANLMSGLVLS IVIKWISFRY
     LVIVAGFSGL FIVGLRFLWQ IIYLSKNKIS HKNTKDRENI VLIGAGDGGS LFMHTYQRHP
     RNEKVIAILD EDPAKRGMNI GGVEVVGSLE KLPALVDGYH VSKAVIAIPS LKPEKYEAIL
     GFCNELGVRV YNMPPVEDVL LGIHQPKGTM REIKISDLLG RKEVELDETA MRKELEGKTI
     LITGAGGSIG SEIVRQVSKH NPAKVILLGH GENSIYLIYH EMIKTKNESM IQYIPIIADI
     QDYERIVEIL KEYQPDIIYH AAAHKHVPLM ESNPVEAFKN NILGTYNVAR AVDQAKVAKM
     VMISTDKAVN PPNIMGATKR VAELIITGMN QQSKSTYCAV RFGNVLGSRG SVVPAFKKQI
     AAGGPVSVTD FRMIRYFMTI PEASQLVIFA GTFSNDGEVF ILDMGEPVKI LDLAKKMILL
     SGHTIEDIGI RETGIRPGEK LYEELLTSSE LVENKLNDQL FVGKVASIPL EETLAFVESL
     KEFVHQPKIM KEKIIKFAND SAKYGG
//
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