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OPGB_SALAR
ID   OPGB_SALAR              Reviewed;         763 AA.
AC   A9MRX7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=SARI_03038;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000880; ABX22879.1; -; Genomic_DNA.
DR   RefSeq; WP_001292735.1; NC_010067.1.
DR   AlphaFoldDB; A9MRX7; -.
DR   SMR; A9MRX7; -.
DR   STRING; 41514.SARI_03038; -.
DR   EnsemblBacteria; ABX22879; ABX22879; SARI_03038.
DR   KEGG; ses:SARI_03038; -.
DR   HOGENOM; CLU_023986_1_0_6; -.
DR   OMA; AMNNTAY; -.
DR   OrthoDB; 1067869at2; -.
DR   UniPathway; UPA00637; -.
DR   Proteomes; UP000002084; 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_1000084494"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01070"
SQ   SEQUENCE   763 AA;  85137 MW;  BDC258F690C705CF CRC64;
     MSELLSVALF LASVLVYAWK AGRNTWWFAA TLTVLGLFVI LNITRYASDY FTGDGINDAV
     LYTLTNSLTG AGVGKYILPG IGIVLALVGV FGALGWILRR RRHHPHHVGY SLLALLLALG
     SVDASPAFRQ ITELVKSQTR DGDPDFAVYY KEPAKTIPNP KLNLVYIYGE SLERTYFDND
     AFPNLTPELG ALKNEGLDFS HTMQLPGTDY TIAGMVASQC GIPLFAPFEG NASASVSSFF
     PQNICLGDIL KNAGYQNYFV QGANLRFAGK DVFLKSHGFD HLYGAEELKT VVTDPSYRND
     WGFYDDTVLD EAWKKFEALS RSGQRFSLFT LTVDTHHPDG FISRTCNRKR YDYDSKPNQS
     FSAVSCSQEN IARFINKIKA SPWFKDTVIV VSSDHLAMNN TAWKYLNKQD RNNLFFILRG
     DKPQQETLAV KRNTMDNGAT VLDILGGDNF IGLGRSSLSG QSLSEVFLNV KEKVLAMKPD
     IVRLWNFPKE MKAFTIDQDK NMIAFSGSHF RLPLLLRVSD KRVEPLPESE YSAPLRFQLA
     DFAPRDNFVW VDRCYKMAQL WAPELALSTD WCVSQGQLGG QQTVQHVDKT QWKGKTAFKD
     TVIDMQRYKG NVDTLKIVDN DIRYKADSFI FNVAGAPEEV KQFSGISRPE TWGRWSNAQL
     GDEVKIEYKA PLPKKFDLVI TAKAFGDNAN RPIPVRVGNE EQTLVLGHDV STTTLHFNNP
     TDASTLVIAP PVPVSTNEGN ILGHSPRKLG IGMVEIKVVN AES
 
 
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