OPGB_SHIFL
ID OPGB_SHIFL Reviewed; 763 AA.
AC Q83IH7;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=SF4390, S4660;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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 -!- SEQUENCE CAUTION:
CC Sequence=AAN45805.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP19583.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN45805.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP19583.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_710098.4; NC_004337.2.
DR RefSeq; WP_001292683.1; NZ_WPGW01000045.1.
DR AlphaFoldDB; Q83IH7; -.
DR SMR; Q83IH7; -.
DR STRING; 198214.SF4390; -.
DR EnsemblBacteria; AAN45805; AAN45805; SF4390.
DR EnsemblBacteria; AAP19583; AAP19583; S4660.
DR GeneID; 1025058; -.
DR KEGG; sfl:SF4390; -.
DR KEGG; sfx:S4660; -.
DR PATRIC; fig|198214.7.peg.5176; -.
DR HOGENOM; CLU_023986_1_0_6; -.
DR OrthoDB; 1067869at2; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..763
FT /note="Phosphoglycerol transferase I"
FT /id="PRO_0000213064"
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 105..127
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
SQ SEQUENCE 763 AA; 85454 MW; 87AC561161B7F7D8 CRC64;
MSELLSFALF LASVLIYAWK AGRNTWWFAA TLTVLGLFVV LNITLFASDY FTGDGINDAV
LYTLTNSLTG AGVSKYILPG IGIVLGLTAV FGALGWILRR RRHHPHHFGY SLLALLLALG
SVDASPAFRQ ITELVKSQSR DGDPDFAAYY KEPSKTIPDP KLNLVYIYGE SLERTYFDNE
AFPDLTPELG ALKNEGLDFS HTQQLPGTDY TIAGMVASQC GIPLFAPFEG NASASVSSFF
PQNICLGDIL KNSGYQNYFV QGANLRFAGK DVFLKSHGFD HLYGSEELKS VVADPHYRND
WGFYDDTVLD EAWKKFEELS RSGQRFSLFT LTVDTHHPDG FISRTCNRKK YDFDGKPNQS
FSAVSCSQEN IATFINKIKA SPWFKDTVIV VSSDHLAMNN TAWKYLNKQD RNNLFFVIRG
DKPQQKTLAV KRNTMDNGAT VLDILGGDNY LGLGRSSLSG QSMSEIFLNI KEKTLAWKPD
IIRLWKFPKE MKEFTIDQQK NMIAFSGSHF RLPLLLRVSD KRVEPLPESE YSAPLRFQLA
DFAPRDNFVW VDSCYKMAQL WAPELALSTD WCVSQGQLGG QQIVQHVDKT TWKSKTAFKD
TVIDMARYKG NVDTLKIVDN DIRYKADSFI FNVAGAPEEV KQFSGISRPE SWGRWSNAQL
GDEVKIEYKH PLPKKFDLVI TAKAYGNNAS RPIPVRVGNE EQTLVLGNEV TTTTLHFDNP
TDADTLVIVP PEPVSTNEGN ILGHSPRKLG IGMVEIKVVE REG
