ID   OPGB_XANCB              Reviewed;         702 AA.
AC   B0RMT0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=opgB {ECO:0000255|HAMAP-Rule:MF_01070};
GN   OrderedLocusNames=xcc-b100_0434;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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; AM920689; CAP49765.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RMT0; -.
DR   SMR; B0RMT0; -.
DR   KEGG; xca:xcc-b100_0434; -.
DR   HOGENOM; CLU_390221_0_0_6; -.
DR   OMA; MDTHHPA; -.
DR   UniPathway; UPA00637; -.
DR   Proteomes; UP000001188; 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..702
FT                   /note="Phosphoglycerol transferase I"
FT                   /id="PRO_1000136634"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
SQ   SEQUENCE   702 AA;  77838 MW;  1E3FC1F3E3C5D93E CRC64;
     MHWILALSLL LLLWLLVASP RLAWLKAGLL SLLLLLLSAW GLVDRLSGDG INAATLYHLR
     ADMDGAGVSD FSGYIAVFIG MVLLSLSPLM LLRVRRFRRP RGGGAVFGAF VVMLLVSMAV
     SPVYRDGKRL YYQLRPVDYA TVVPEYQVPQ QPLQKRKNIV WIYGESLERT YFDEATFPGL
     MPNLRQLATE AVDVRNLTST EGSGWTIAGM VASMCGVPLT TAPGDENSMG RMGLFLPEAR
     CLGDYLKDQG YRNHYVGGAD ASFAGKGSFL ASHGFDVVHD VNYFHDKGVA PKHFSAWGVH
     DDVLLDDAWE SFQTLSRAGQ PFMLTTLTMD THHPAGHLPL ACKNQRYESP LGDIGLLHAI
     KCSDRLIGEL VTRIRNSRYG RNTIIVIASD HLAMPNDLSD VLAKQKRENL LLFLGKDIPP
     QQVVRRAGST LDSGATLLQL LEPGMRTLGF GRSLLANDAP PSASVAASRD SGRDYPRYLA
     YARTLWTGRS TRMLRVNGNG DVVVGVQQVR PPVLLEYDDD TNLKTVYLEN TSRQFDRTHS
     DGTLAYVDRC TAFEDGSADG DWCALVVDRN QHMKLYRDPD LTRGIAVDAP LDVTPQAPRP
     RVRQPIMLTQ AARKTEAGRY MLELYAKRRP TRAFWVEAVS SERKVVLAQQ WVVPDASGRI
     RMPVGLEHAV EDLGIRAWLD YTEEVSVDDL ALVKDTAVAD RS