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 27-MAR-2024, entry version 113.
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; Pseudomonadota; 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 GeneID; 66909632; -.
DR KEGG; xac:XAC0421; -.
DR eggNOG; COG1368; Bacteria.
DR HOGENOM; CLU_390221_0_0_6; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000000576; Chromosome.
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:0009250; P:glucan biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd16015; LTA_synthase; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 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 PANTHER; PTHR47371; LIPOTEICHOIC ACID SYNTHASE; 1.
DR PANTHER; PTHR47371:SF3; PHOSPHOGLYCEROL TRANSFERASE I; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 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
//
