OPGB_ECO55
ID OPGB_ECO55 Reviewed; 763 AA.
AC B7LE10;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=EC55989_5021;
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928145; CAV02143.1; -; Genomic_DNA.
DR RefSeq; WP_001292687.1; NC_011748.1.
DR AlphaFoldDB; B7LE10; -.
DR SMR; B7LE10; -.
DR EnsemblBacteria; CAV02143; CAV02143; EC55989_5021.
DR KEGG; eck:EC55989_5021; -.
DR HOGENOM; CLU_023986_1_0_6; -.
DR OMA; AMNNTAY; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000000746; 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_1000149751"
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; 85494 MW; 6B5130DB9618CA09 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 RSSQRFSLFT LTVDTHHPDG FISRTCNRKK YDFDGKPNQS
FSAVSCSQEN IAAFINKIKA SPWFKDTVIV VSSDHLAMNN TAWKYLNKQD RNNLFFVIRG
DKPQQETLAV KRNTMDNGAT VLDILGGDNY LGLGRSSLSG QSMSEIFLNI KEKTLAWKPD
IIRLWKFPKE MKEFTIDQQK NMIAFSGSHF RLPLLLRVSD KRVEPLPESE YSAPLRFQLA
DFAPRDNFVW VDRCYKMAQL WAPELALSTD WCVSQGQLGG QQIVQHVDKT TWQGKTAFKD
TVIDMARYKG NVDTLKIVDN DIRYKADSFI FNVAGAPEEV KQFSGISRPE SWGRWSNAQL
GDEVKIEYKH PLPKKFDLVI TAKAYGNNAS RPIPVRVGNE EQTLVLGNEV TTTTLHFDNP
TDADTLVIVP PEPVSTNEGN ILGHSPRKLG IGMVEIKVVE REG