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YBJG_ECOLI
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   03-AUG-2022, entry version 141.
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; Proteobacteria; 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}.
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DR   EMBL; U00096; AAC73928.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35544.1; -; 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; P75806; -.
DR   PRIDE; P75806; -.
DR   EnsemblBacteria; AAC73928; AAC73928; b0841.
DR   EnsemblBacteria; BAA35544; BAA35544; BAA35544.
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; FLFWHRV; -.
DR   PhylomeDB; P75806; -.
DR   BioCyc; EcoCyc:G6439-MON; -.
DR   BioCyc; MetaCyc:G6439-MON; -.
DR   PRO; PR:P75806; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   InterPro; IPR033879; UPP_Pase.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 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
 
 
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