ID   OPGB_SALDC              Reviewed;         763 AA.
AC   B5FTA1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Phosphoglycerol transferase I {ECO:0000255|HAMAP-Rule:MF_01070};
DE            EC=2.7.8.20 {ECO:0000255|HAMAP-Rule:MF_01070};
DE   AltName: Full=Phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase {ECO:0000255|HAMAP-Rule:MF_01070};
GN   Name=mdoB {ECO:0000255|HAMAP-Rule:MF_01070};
GN   Synonyms=opgB {ECO:0000255|HAMAP-Rule:MF_01070};
GN   OrderedLocusNames=SeD_A4955;
OS   Salmonella dublin (strain CT_02021853).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT_02021853;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- FUNCTION: Transfers a phosphoglycerol residue from phosphatidylglycerol
CC       to the membrane-bound nascent glucan backbones. {ECO:0000255|HAMAP-
CC       Rule:MF_01070}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphatidylglycerol + membrane-derived-oligosaccharide D-
CC         glucose = 1,2-diacyl-sn-glycerol + membrane-derived-oligosaccharide
CC         6-(glycerophospho)-D-glucose.; EC=2.7.8.20;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01070};
CC   -!- PATHWAY: Glycan metabolism; osmoregulated periplasmic glucan (OPG)
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01070}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01070}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01070}.
CC   -!- SIMILARITY: Belongs to the OpgB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01070}.
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DR   EMBL; CP001144; ACH74498.1; -; Genomic_DNA.
DR   RefSeq; WP_001292722.1; NC_011205.1.
DR   AlphaFoldDB; B5FTA1; -.
DR   SMR; B5FTA1; -.
DR   KEGG; sed:SeD_A4955; -.
DR   HOGENOM; CLU_023986_1_0_6; -.
DR   OMA; AMNNTAY; -.
DR   UniPathway; UPA00637; -.
DR   Proteomes; UP000008322; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008960; F:phosphatidylglycerol-membrane-oligosaccharide glycerophosphotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR   GO; GO:0009250; P:glucan biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.720.10; -; 1.
DR   HAMAP; MF_01070; MdoB_OpgB; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR020881; OpgB.
DR   InterPro; IPR000917; Sulfatase_N.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..763
FT                   /note="Phosphoglycerol transferase I"
FT                   /id="PRO_1000136629"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
SQ   SEQUENCE   763 AA;  84999 MW;  53ED1D14C21BF79E CRC64;
     MSELLSVALF LASVLIYAWK AGRNTWWFAA TLTVLGLFVI LNITLYASDY FTGDGINDAV
     LYTLTNSLTG AGVGKYILPG IGIALALVAV FGALGWVLRR RRHHPHHVGY SLLALLLALG
     SVDASPAFRQ ITELVKSQMR DGDPDFAVYY KEPAKTIPNP KLNLVYIYGE SLERTYFDND
     AFPNLTPELG ALKNEGLDFS HTMQLPGTDY TIAGMVASQC GIPLFAPFEG NASASVSSFF
     PQNICLGDIL KNSGYQNYFV QGANLRFAGK DVFLKSHGFD HLYGAEELKT VVADPSYRND
     WGFYDDTVLD EAWKKFEALS RSGQRFSLFT LTVDTHHPDG FISRTCNRKR YDYDGKPNQS
     FSAVSCSQEN IAEFINKIKA SPWFKDTVIV VSSDHLAMNN TAWKYLNKQD RNNLFFILRG
     DKPQQETLAV KRNTMDNGAT VLDILGGDNF IGLGRSSLSG QSLSEVFLNV KEKVLAMKPD
     IIRLWNFPKE IKDFTVDRDK NMIAFSGSHF RLPLLLRVSD KRVEPLPESE YSAPLRFQLA
     DFAPRDNFVW IDRCYKMAQL WAPALALSTD WCVSQGQLGG QQTVQHVDKA QWKGKTAFKE
     TVIDVTRYQG NVDTLKIVDN DIRYKADSFI FNVAGAPEEV KQFSGISRPE SWGRWSNAQL
     GDEVKIEYKA PLPKKFDLVI TAKAFGDNAN RPIPVRVGNE EQTLVLGHDV STITLHFNNP
     TDANTLVIAP PAPVSTNEGN ILGHSPRKLG IGMVEIKVVN VES