OPGB_ECOLI
ID OPGB_ECOLI Reviewed; 763 AA.
AC P39401; Q2M5V7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Phosphoglycerol transferase I;
DE EC=2.7.8.20;
DE AltName: Full=Phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase;
GN Name=mdoB; Synonyms=opgB, yjjO; OrderedLocusNames=b4359, JW5794;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION.
RX PubMed=6094515; DOI=10.1128/jb.160.3.976-981.1984;
RA Jackson B.J., Bohin J.-P., Kennedy E.P.;
RT "Biosynthesis of membrane-derived oligosaccharides: characterization of
RT mdoB mutants defective in phosphoglycerol transferase I activity.";
RL J. Bacteriol. 160:976-981(1984).
RN [5]
RP FUNCTION.
RX PubMed=2985566; DOI=10.1016/s0021-9258(18)89142-6;
RA Fiedler W., Rotering H.;
RT "Characterization of an Escherichia coli mdoB mutant strain unable to
RT transfer sn-1-phosphoglycerol to membrane-derived oligosaccharides.";
RL J. Biol. Chem. 260:4799-4806(1985).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Transfers a phosphoglycerol residue from phosphatidylglycerol
CC to the membrane-bound nascent glucan backbones.
CC {ECO:0000269|PubMed:2985566, ECO:0000269|PubMed:6094515}.
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 -!- PATHWAY: Glycan metabolism; osmoregulated periplasmic glucan (OPG)
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the OpgB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97258.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97258.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77315.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78349.1; -; Genomic_DNA.
DR PIR; S56586; S56586.
DR RefSeq; NP_418779.2; NC_000913.3.
DR RefSeq; WP_001292679.1; NZ_LN832404.1.
DR AlphaFoldDB; P39401; -.
DR SMR; P39401; -.
DR BioGRID; 4261390; 165.
DR DIP; DIP-10175N; -.
DR IntAct; P39401; 1.
DR STRING; 511145.b4359; -.
DR jPOST; P39401; -.
DR PaxDb; P39401; -.
DR PRIDE; P39401; -.
DR EnsemblBacteria; AAC77315; AAC77315; b4359.
DR EnsemblBacteria; BAE78349; BAE78349; BAE78349.
DR GeneID; 948888; -.
DR KEGG; ecj:JW5794; -.
DR KEGG; eco:b4359; -.
DR PATRIC; fig|1411691.4.peg.2327; -.
DR EchoBASE; EB2476; -.
DR eggNOG; COG1368; Bacteria.
DR HOGENOM; CLU_023986_1_0_6; -.
DR OMA; AMNNTAY; -.
DR PhylomeDB; P39401; -.
DR BioCyc; EcoCyc:PGLYCEROLTRANSI-MON; -.
DR BioCyc; MetaCyc:PGLYCEROLTRANSI-MON; -.
DR UniPathway; UPA00637; -.
DR PRO; PR:P39401; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0004065; F:arylsulfatase activity; IBA:GO_Central.
DR GO; GO:0008960; F:phosphatidylglycerol-membrane-oligosaccharide glycerophosphotransferase activity; IDA:EcoCyc.
DR GO; GO:0009250; P:glucan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IDA:EcoCyc.
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; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..763
FT /note="Phosphoglycerol transferase I"
FT /id="PRO_0000213059"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 763 AA; 85494 MW; 4F6C46DE859E7D65 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 TWQGKTAFKD
TVIDMARYKG NVDTLKIVDN DIRYKADSFI FNVAGAPEEV KQFSGISRPE SWGRWSNAQL
GDEVKIEYKH PLPKKFDLVI TAKAYGNNAS RPIPVRVGNE EQTLVLGNEV TTTTLHFDNP
TDADTLVIVP PEPVSTNEGN ILGHSPRKLG IGMVEIKVVE REG
