ID   UPPP1_CORJK             Reviewed;         281 AA.
AC   Q4JXD8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Undecaprenyl-diphosphatase 1;
DE            EC=3.6.1.27;
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase 1;
DE   AltName: Full=Bacitracin resistance protein 1;
GN   Name=uppP1; OrderedLocusNames=jk0367;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B.,
RA   Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T.,
RA   Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P.,
RA   Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant
RT   nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring
RT   bacterium of the human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl
CC       diphosphate (UPP). Confers resistance to bacitracin (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Undecaprenyl diphosphate + H(2)O =
CC       undecaprenyl phosphate + phosphate.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
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   -!- SIMILARITY: Belongs to the uppP family.
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DR   EMBL; CR931997; CAI36519.1; -; Genomic_DNA.
DR   RefSeq; YP_250137.1; -.
DR   GeneID; 3433526; -.
DR   GenomeReviews; CR931997_GR; jk0367.
DR   KEGG; cjk:jk0367; -.
DR   NMPDR; fig|306537.3.peg.1468; -.
DR   HOGENOM; Q4JXD8; -.
DR   OMA; Q4JXD8; LPDAFDP.
DR   BioCyc; CJEI306537:JK0367-MON; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:HAMAP.
DR   GO; GO:0007047; 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-KW.
DR   HAMAP; MF_01006; -; 1.
DR   InterPro; IPR003824; Bacitracin-R_BacA.
DR   Pfam; PF02673; BacA; 1.
DR   TIGRFAMs; TIGR00753; undec_PP_bacA; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Hydrolase;
KW   Membrane; Peptidoglycan synthesis; Transmembrane.
FT   CHAIN         1    281       Undecaprenyl-diphosphatase 1.
FT                                /FTId=PRO_0000227615.
FT   TRANSMEM     95    115       Potential.
FT   TRANSMEM    119    139       Potential.
FT   TRANSMEM    152    172       Potential.
FT   TRANSMEM    195    215       Potential.
FT   TRANSMEM    227    247       Potential.
FT   TRANSMEM    256    276       Potential.
SQ   SEQUENCE   281 AA;  30422 MW;  0CFF3F6080F25A31 CRC64;
     MTDPATTMSW VQVIVLSVVQ GLTEFLPVSS SGHLRIVSQL FWGEDAGASF TAVIQLGTEL
     AVLVFFAKDI WRILTAWFAG LADKSKRNFD YRMGWMVIAG TIPVGLAGVL LKDLIRENFR
     NLWITATVLI LFSLVFILAE RRGKKTRGFE ELTMKDAVLM GLWQCLALIP GVSRSGGTIS
     GGLFLNLDRE VATRFSFLLA IPAVLASGLF SLPDAFDPQA GQAASGLQLL VGSGIGFVVG
     YISIAWLLKF VSNHSFAWFA AYRIPLGLLV MALLGTGVMA A
//