ID   OPGB_XANCP              Reviewed;         702 AA.
AC   Q8PDD7;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 2.
DT   03-AUG-2022, entry version 102.
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}; Synonyms=mdoB;
GN   OrderedLocusNames=XCC0403;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAM39721.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008922; AAM39721.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_635797.2; NC_003902.1.
DR   RefSeq; WP_011035656.1; NC_003902.1.
DR   AlphaFoldDB; Q8PDD7; -.
DR   SMR; Q8PDD7; -.
DR   STRING; 340.xcc-b100_0434; -.
DR   EnsemblBacteria; AAM39721; AAM39721; XCC0403.
DR   KEGG; xcc:XCC0403; -.
DR   PATRIC; fig|190485.4.peg.441; -.
DR   eggNOG; COG1368; Bacteria.
DR   HOGENOM; CLU_390221_0_0_6; -.
DR   OMA; MDTHHPA; -.
DR   UniPathway; UPA00637; -.
DR   Proteomes; UP000001010; 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; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..702
FT                   /note="Phosphoglycerol transferase I"
FT                   /id="PRO_0000213066"
FT   TRANSMEM        3..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
FT   TRANSMEM        73..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
FT   TRANSMEM        102..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
SQ   SEQUENCE   702 AA;  77682 MW;  2F07C42CF0A435E3 CRC64;
     MHWILALSLL LLLLLLVASP RLAWLKAGLL SLLLLLLSAW GLVDRLSGDG VNAATLYHLR
     ADMDGAGVSD FSGYIAVFIG MVLLSLSPLV LLRVRRFRRP RGGGAVFGAF VVMLLVSVAV
     SPLYRDGKRL YYQLRPVDYA TVVPEYQVPQ QPLQKRKNIV WIYGESLERT YFDEATFPGL
     MPNLHQLATE AVDVRNLTST EGSGWTIAGM VASMCGVPLT TAPGDENSMG RMGLFLPEAR
     CLGDYLKDQG YRNHYVGGAD ASFAGKGSFL ASHGFDVVHD VNYFHDKGVA PKHFSAWGVH
     DDVLLDDAWD SFQTLSRAGQ PFMLTTLTMD THHPAGHLPL ACKNQRYESP LGDIGLLHAI
     KCSDRLIGRL VTRIRNSRYG RNTIIVIASD HLAMPNDLSD VLAKQKRENL LLFLGKDIPP
     QQVVTRAGST LDSGATLLQL LEPGMRTLGF GRSLLANDAP PSASVAASRD SGKNYPRYLA
     YARTLWTGRS TRMLRVNGNG DVVVGVQQVR PPVLLEYDDN TNLKTVYLEN TSRQFDRTHS
     DGTLAYVDRC TAFEDGSADG DWCALVVDRN QHMKLYRDPD LTRGIAVDAP LDVTPQAPRP
     RVRQPIMLTQ AARKTEAGRY MLELYAKRRP TRAFWVEAVS SERKVVLAQQ WVVPDASGRI
     RMPVGLEHAV EDLEIRAWLD YTEEVSVDDL ALVKDTAVAD RS