ID   OPGB_ECOUT              Reviewed;         763 AA.
AC   Q1R2E6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=UTI89_C5065;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE10468.1; -; Genomic_DNA.
DR   RefSeq; WP_001292631.1; NC_007946.1.
DR   AlphaFoldDB; Q1R2E6; -.
DR   SMR; Q1R2E6; -.
DR   EnsemblBacteria; ABE10468; ABE10468; UTI89_C5065.
DR   KEGG; eci:UTI89_C5065; -.
DR   HOGENOM; CLU_023986_1_0_6; -.
DR   OMA; AMNNTAY; -.
DR   UniPathway; UPA00637; -.
DR   Proteomes; UP000001952; 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_1000064575"
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;  85464 MW;  111C5D1C01604D43 CRC64;
     MSELLSFALF LASVLIYAWK AGRNTWWFAA TLTVLGLFVV LNITLFASDY FTGDGINDAV
     LYTLTNSLTG AGVSKYILPG IGIVLGLAAV FGALGWILRR RRHHPHHFGY SLLALLLALG
     SVDASPAFRQ ITELVKSQSR DGDPDFAAYY KEPSKTIPDP KLNLVYIYGE SLERTYFDNE
     AFPDLTPELG ALKNEGLDFS HTQQLPGTDY TIAGMVASQC GIPLFAPFEG NASASVSSFF
     PQNICLGDIM KNSGYQNYFV QGANLRFAGK DVFLKSHGFD HLYGSEELKS VVADPHYRND
     WGFYDDTVLD EAWKKFEELS RSGQRFSLFT LTVDTHHPDG FISRTCNRKK YDFDGKPNQS
     FSAVSCSQEN IATFINKIKA SPWFKDTVIV VSSDHLAMNN TAWKYLNKQD RNNLFFVIRG
     DKPQQETLAV KRNTMDNGAT VLDILGGDNY LGLGRSSLSG QSMSEIFLNI KEKTLAWKPD
     IIRLWKFPKE MKEFTIDQQK NMIAFSGSHF RLPLLLRVSD KRVEPLPESE YSAPLRFQLA
     DFAPRDNFVW VDRCYKMAQL WAPELALSTD WCVSQGQLGG QQIVQHVDKA IWKGKTAFKD
     TVIDMARYKG NVDTLKIVDN DIRYKADSFI FNVAGAPEEV KQFSGISRPE SWGRWSNAQL
     GDEVKIEYKH PLPKKFDLVI TAKAYGNNAS RPIPVRVGNE EQTLVLGNEV TTTTLHFDNP
     TDADTLVIVP PEPVSTNEGN ILGHSPRKLG IGMVEIKVVE REG