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Database: UniProt
Entry: D6IHR8_ECOLX
LinkDB: D6IHR8_ECOLX
Original site: D6IHR8_ECOLX 
ID   D6IHR8_ECOLX            Unreviewed;       763 AA.
AC   D6IHR8;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Phosphoglycerol transferase I {ECO:0000256|HAMAP-Rule:MF_01070};
DE            EC=2.7.8.20 {ECO:0000256|HAMAP-Rule:MF_01070};
DE   AltName: Full=Phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase {ECO:0000256|HAMAP-Rule:MF_01070};
GN   Name=mdoB {ECO:0000256|HAMAP-Rule:MF_01070};
GN   Synonyms=opgB {ECO:0000256|HAMAP-Rule:MF_01070};
GN   ORFNames=ECDG_02753 {ECO:0000313|EMBL:EFF03549.2};
OS   Escherichia coli B185.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=550676 {ECO:0000313|EMBL:EFF03549.2, ECO:0000313|Proteomes:UP000004669};
RN   [1] {ECO:0000313|EMBL:EFF03549.2, ECO:0000313|Proteomes:UP000004669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B185 {ECO:0000313|EMBL:EFF03549.2,
RC   ECO:0000313|Proteomes:UP000004669};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Escherichia coli B185.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers a phosphoglycerol residue from phosphatidylglycerol
CC       to the membrane-bound nascent glucan backbones. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01070};
CC   -!- PATHWAY: Glycan metabolism; osmoregulated periplasmic glucan (OPG)
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01070}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01070}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01070}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the OpgB family. {ECO:0000256|HAMAP-
CC       Rule:MF_01070}.
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DR   EMBL; GG749190; EFF03549.2; -; Genomic_DNA.
DR   RefSeq; WP_001292676.1; NZ_GG749190.1.
DR   AlphaFoldDB; D6IHR8; -.
DR   SMR; D6IHR8; -.
DR   UniPathway; UPA00637; -.
DR   Proteomes; UP000004669; Unassembled WGS sequence.
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:0009250; P:glucan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd16015; LTA_synthase; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 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   PANTHER; PTHR47371; LIPOTEICHOIC ACID SYNTHASE; 1.
DR   PANTHER; PTHR47371:SF3; PHOSPHOGLYCEROL TRANSFERASE I; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW   Rule:MF_01070};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01070};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01070};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01070};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01070};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01070}.
FT   TRANSMEM        28..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01070"
FT   TRANSMEM        80..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01070"
FT   TRANSMEM        110..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01070"
FT   DOMAIN          163..446
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
SQ   SEQUENCE   763 AA;  85524 MW;  286AC006F389EAA7 CRC64;
     MSELLSFALF LASVLIYAWK AGRNTWWFAA TLTVLGLFVV LNITLFASDY FTGDGINDAV
     LYTLTNSLTG AGVSKYILPG IGIVLGLTAV FGALGWILRR RRHHPHHFGY SLLALLLALG
     SVDASPAFRQ ITELVKSQSR DGDPDFAAYY KEPSKTIPDP KLNLVYIYGE SLERTYFDNE
     AFPDLTPELG ALKNEGLDFS HTQQLPGTDY TIAGMVASQC GIPLFAPFEG NASASVSSFF
     PQNICLGDIL 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 QQIVQHVDKT TWKSKTAFKD
     TVIDMARYKG NVDTLKIVDN DIRYKADSFI FNVAGAPEEV KQFSGISRPE SWGRWSNAQL
     GDEVKIEYKH PLPKKFDLVI TAKAYGNNAS RPIPVRVGNE EQTLVLGNEV TTTTLHFDNP
     TDADTLVIVP PEPVSTNEGN ILGHSPRKLG IGMVEIKVVE REG
//
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