ID YBJG_ECOLI Reviewed; 198 AA. AC P75806; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 149. DE RecName: Full=Putative undecaprenyl-diphosphatase YbjG; DE EC=3.6.1.27; DE AltName: Full=Undecaprenyl pyrophosphate phosphatase; GN Name=ybjG; OrderedLocusNames=b0841, JW5112; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., RA Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP FUNCTION. RX PubMed=15778224; DOI=10.1074/jbc.m412277200; RA El Ghachi M., Derbise A., Bouhss A., Mengin-Lecreulx D.; RT "Identification of multiple genes encoding membrane proteins with RT undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia RT coli."; RL J. Biol. Chem. 280:18689-18695(2005). RN [5] RP TOPOLOGY [LARGE SCALE ANALYSIS]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=15919996; DOI=10.1126/science.1109730; RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.; RT "Global topology analysis of the Escherichia coli inner membrane RT proteome."; RL Science 308:1321-1323(2005). CC -!- FUNCTION: Overexpression leads to increased undecaprenyl diphosphatase CC activity and to increased resistance to bacitracin. May have a CC preferred substrate other than undecaprenyl diphosphate in vivo. CC {ECO:0000269|PubMed:15778224}. CC -!- CATALYTIC ACTIVITY: CC Reaction=di-trans,octa-cis-undecaprenyl diphosphate + H2O = di- CC trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate; CC Xref=Rhea:RHEA:28094, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58405, ChEBI:CHEBI:60392; EC=3.6.1.27; CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the BcrC/YbjG family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U00096; AAC73928.1; -; Genomic_DNA. DR EMBL; AP009048; BAA35544.2; -; Genomic_DNA. DR PIR; A64822; A64822. DR RefSeq; NP_415362.1; NC_000913.3. DR RefSeq; WP_001295291.1; NZ_SSZK01000002.1. DR AlphaFoldDB; P75806; -. DR SMR; P75806; -. DR BioGRID; 4262827; 184. DR STRING; 511145.b0841; -. DR PaxDb; 511145-b0841; -. DR EnsemblBacteria; AAC73928; AAC73928; b0841. DR GeneID; 945450; -. DR KEGG; ecj:JW5112; -. DR KEGG; eco:b0841; -. DR PATRIC; fig|1411691.4.peg.1437; -. DR EchoBASE; EB3440; -. DR eggNOG; COG0671; Bacteria. DR InParanoid; P75806; -. DR OMA; VYMGVHY; -. DR OrthoDB; 9801622at2; -. DR PhylomeDB; P75806; -. DR BioCyc; EcoCyc:G6439-MONOMER; -. DR BioCyc; MetaCyc:G6439-MONOMER; -. DR PRO; PR:P75806; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc. DR GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IDA:EcoCyc. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc. DR CDD; cd03385; PAP2_BcrC_like; 1. DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1. DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf. DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase. DR InterPro; IPR033879; UPP_Pase. DR PANTHER; PTHR14969; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1. DR PANTHER; PTHR14969:SF60; UNDECAPRENYL-DIPHOSPHATASE YBJG-RELATED; 1. DR Pfam; PF01569; PAP2; 1. DR SMART; SM00014; acidPPc; 1. DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1. PE 1: Evidence at protein level; KW Antibiotic resistance; Cell inner membrane; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Hydrolase; Membrane; KW Peptidoglycan synthesis; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..198 FT /note="Putative undecaprenyl-diphosphatase YbjG" FT /id="PRO_0000168739" FT TOPO_DOM 1..27 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 28..48 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 49..57 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 58..78 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 79..120 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 121..143 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 144..149 FT /note="Periplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 150..172 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 173..198 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" SQ SEQUENCE 198 AA; 22399 MW; A1ED7A934F78A15D CRC64; MLENLNLSLF SLINATPDSA PWMISLAIFI AKDLITVVPL LAVVLWLWGL TAQRQLVIKI AIALAVSLFV SWTMGHLFPH DRPFVENIGY NFLHHAADDS FPSDHGTVIF TFALAFLCWH RLWSGSLLMV LAVVIAWSRV YLGVHWPLDM LGGLLAGMIG CLSAQIIWQA MGHKLYQRLQ SWYRVCFALP IRKGWVRD //