OPGB_SALTI
ID OPGB_SALTI Reviewed; 763 AA.
AC Q8Z0W2;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=STY4894, t4584;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL513382; CAD03379.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO72019.1; -; Genomic_DNA.
DR RefSeq; NP_458956.1; NC_003198.1.
DR RefSeq; WP_001292715.1; NZ_WSUR01000014.1.
DR AlphaFoldDB; Q8Z0W2; -.
DR SMR; Q8Z0W2; -.
DR STRING; 220341.16505648; -.
DR EnsemblBacteria; AAO72019; AAO72019; t4584.
DR KEGG; stt:t4584; -.
DR KEGG; sty:STY4894; -.
DR PATRIC; fig|220341.7.peg.5015; -.
DR eggNOG; COG1368; Bacteria.
DR HOGENOM; CLU_023986_1_0_6; -.
DR OMA; AMNNTAY; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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_0000213062"
FT TRANSMEM 4..19
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
FT TRANSMEM 26..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
FT TRANSMEM 76..98
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
FT TRANSMEM 110..132
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
SQ SEQUENCE 763 AA; 85130 MW; 9A53BDCFEF75EFAD CRC64;
MSELLSVALF LASVLIYAWK AGRNTWWFAA TLTVLGLFVI LNITLYASDY FTGDGINDAV
LYTLTNSLTG AGVGKYILPG IGIALALVAV FGALGWVLRR RRHHPHHVGY SLLALLLALG
SVDASPAFRQ ITELVKSQMR DGDPDFAVYY KEPAKTIPHP KLNLVYIYGE SLERTYFDND
AFPNLTPELG ALKNEGLDFS HTMQLPGTDY TIAGMVASQC GIPLFAPFEG NASASVSSFF
PQNICLGDIL KNSGYQNYFV QGANLRFAGK DVFLKSHGFD HLYGAEELKT VVADPSYRND
WGFYDDTVLD EAWKKFEALS RSGQRFSLFT LTVDTHHPDG FISRTCNRKR YDYDGKPNQS
FSTVSCSQEN IAEFINKIKA SPWFKDTVIV VSSDHLAMNN TAWKYLNKQD RNNLFFILRG
DKPQQETLAV KRNTMDNGAT VLDILGGDNF IGLGRSSLSG QSLSEVFLNV KEKVLAMKPD
IIRLWNFPKE IKDFTVDRDK NMIAFSGSHF RLPLLLRVSD KRVEPLPESE YSAPLRFQLA
DFAPRDNFVW IDRCYKMAQL WAPALALSTD WCVSQGQLGG QQTVQHVDKA QWQGKTAFKD
TMIDMERYKG NVDTLKIVDN DIRYKADSFI FNVAGAPEEV KQFSGISRPE SWGRWSNAQL
GDEVKIEYKA PLPKKFDLVI TAKAFGDNAN RPIPVRVGNE EQTLVLGHDV STITLHFNNP
TDANTLVIAP PAPVSTNEGN ILGHSPRKLG IGMVEIKVVN VES
