(data stored in ACNUC7421 zone)

SWISSPROT: C5BHG4_EDWI9

ID   C5BHG4_EDWI9            Unreviewed;       272 AA.
AC   C5BHG4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 56.
DE   RecName: Full=Undecaprenyl-diphosphatase {ECO:0000256|HAMAP-Rule:MF_01006};
DE            EC=3.6.1.27 {ECO:0000256|HAMAP-Rule:MF_01006};
DE   AltName: Full=Bacitracin resistance protein {ECO:0000256|HAMAP-Rule:MF_01006};
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000256|HAMAP-Rule:MF_01006};
GN   Name=uppP {ECO:0000256|HAMAP-Rule:MF_01006};
GN   OrderedLocusNames=NT01EI_0530 {ECO:0000313|EMBL:ACR67763.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67763.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl
CC       diphosphate (UPP). Confers resistance to bacitracin.
CC       {ECO:0000256|HAMAP-Rule:MF_01006}.
CC   -!- CATALYTIC ACTIVITY: Ditrans,octacis-undecaprenyl diphosphate +
CC       H(2)O = ditrans,octacis-undecaprenyl phosphate + phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01006, ECO:0000256|SAAS:SAAS00702352}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01006}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01006}.
CC   -!- MISCELLANEOUS: Bacitracin is thought to be involved in the
CC       inhibition of peptidoglycan synthesis by sequestering undecaprenyl
CC       diphosphate, thereby reducing the pool of lipid carrier available.
CC       {ECO:0000256|HAMAP-Rule:MF_01006}.
CC   -!- SIMILARITY: Belongs to the UppP family. {ECO:0000256|HAMAP-
CC       Rule:MF_01006, ECO:0000256|SAAS:SAAS00702351}.
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DR   EMBL; CP001600; ACR67763.1; -; Genomic_DNA.
DR   RefSeq; WP_015869963.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0530; -.
DR   EnsemblBacteria; ACR67763; ACR67763; NT01EI_0530.
DR   GeneID; 7961555; -.
DR   KEGG; eic:NT01EI_0530; -.
DR   PATRIC; fig|634503.3.peg.480; -.
DR   eggNOG; ENOG4105DWR; Bacteria.
DR   eggNOG; COG1968; LUCA.
DR   HOGENOM; HOG000218356; -.
DR   KO; K06153; -.
DR   OMA; PDARMGW; -.
DR   OrthoDB; POG091H00ZR; -.
DR   Proteomes; UP000001485; 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:0050380; F:undecaprenyl-diphosphatase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
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; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01006; Undec_diphosphatase; 1.
DR   InterPro; IPR003824; UppP.
DR   PANTHER; PTHR30622; PTHR30622; 1.
DR   Pfam; PF02673; BacA; 1.
DR   TIGRFAMs; TIGR00753; undec_PP_bacA; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BHG4.
DR   SWISS-2DPAGE; C5BHG4.
KW   Antibiotic resistance {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702335};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01006};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702333};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702357};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702339};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702354, ECO:0000313|EMBL:ACR67763.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702342};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702374};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702376};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01006,
KW   ECO:0000256|SAAS:SAAS00702360}.
FT   TRANSMEM     49     68       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM     89    109       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM    115    135       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM    194    212       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM    224    245       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
FT   TRANSMEM    251    271       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01006}.
SQ   SEQUENCE   272 AA;  29690 MW;  BFFCDF9AAABEF909 CRC64;
     MDLHTLLNAF ILGIVEGLTE FLPVSSTGHM IIVGHWLGFE GDKAKTFEVI IQLGSILAVV
     VMFWRRLFGL IGIHFGRPVV HEGRGQGQLR LGHIVLAMIP AVVLGLLLHD FIKSLFTPLT
     VAYALVVGGL LLLAAEWLKP AQTRAVGLDD ITYRQAFMIG CFQCLALWPG FSRSGATISG
     GMLMGVSRYA ASEFSFLLAV PMMMGASALE LYKSLPYLSL GDLPMFSVGF VTAFIVALIA
     IKTFLNLIKR ISFVPFAIYR FIVAAAVYLV FC
//

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