ID   OPGB_XANAC              Reviewed;         702 AA.
AC   Q8PQA7;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 2.
DT   03-AUG-2022, entry version 108.
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=XAC0421;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
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=AAM35312.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008923; AAM35312.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011050307.1; NC_003919.1.
DR   AlphaFoldDB; Q8PQA7; -.
DR   SMR; Q8PQA7; -.
DR   STRING; 190486.XAC0421; -.
DR   EnsemblBacteria; AAM35312; AAM35312; XAC0421.
DR   GeneID; 66909632; -.
DR   KEGG; xac:XAC0421; -.
DR   eggNOG; COG1368; Bacteria.
DR   HOGENOM; CLU_390221_0_0_6; -.
DR   OMA; MDTHHPA; -.
DR   UniPathway; UPA00637; -.
DR   Proteomes; UP000000576; 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_0000213065"
FT   TRANSMEM        5..24
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;  77642 MW;  63D35EC27BB2FB45 CRC64;
     MHWMLLVSLL LLLWLLVASP RLAWLKAGLL SLFLLLLSAW GLVDRLSGDG INAATLYHLR
     ADMDGAGVSD FSGYIAVFVG MLLLSLSPLL LVRIRRFQRP RGGGAVFAGF VGMLLVGIAA
     SPLYRDGKRL YYQLRPVDYA TVVPEYQVPQ QPLHKRKNIV WIYGESLERT YFDEQVFPGL
     MPNLRAVATE AVDVRNLAST EGSGWTIAGM VASMCGVPLT TAPGDENSMD RMGMFLPEAR
     CLGDYLKDQG YRNHYVGGAD ASFAGKGRFL SSHGFDVVHD VHYFQDQGVA PKHFSAWGVH
     DDVLLDDAWD TFQTLSRAGQ PFLLTTLTMD THHPAGHLPS ACKGQQYDSP LGDIGLLHAI
     KCSDRLIGEL VARIRNSRYG KNTIIVIASD HLAMPNDLSD VLAKQKRENL LLFLGEDIAP
     QQVVTRAGST LDSGATLLQL LEPGMRTLGF GRSFLASDAP PSASAAASRD SGKDYPRYLA
     YARTLWTGRS TRMLRINGNG DVVVGVQQVR PPVLLEYDKD TNLKTVYLEN TSRQFDRTHS
     KGTLAYVDRC TAFEDGSADG DWCALVVDRH QSMKLYRDPD LARGIAIDAP LEATQQGPRP
     RVRQPIMLTQ AARKTDAGRY MLELYAKRRP TRAFWVEAVS SERKVVLAQQ WVVPDAAGRI
     RMPVGLEHAV EDLEIRAWLD YTEDVSVDDL ALVKDIPVAD RS