ID   UPPP2_CORJK             Reviewed;         290 AA.
AC   Q4JVN6;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Undecaprenyl-diphosphatase 2;
DE            EC=3.6.1.27;
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase 2;
DE   AltName: Full=Bacitracin resistance protein 2;
GN   Name=uppP2; OrderedLocusNames=jk0957;
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; CAI37121.1; -; Genomic_DNA.
DR   RefSeq; YP_250739.1; -.
DR   GeneID; 3433525; -.
DR   GenomeReviews; CR931997_GR; jk0957.
DR   KEGG; cjk:jk0957; -.
DR   NMPDR; fig|306537.3.peg.417; -.
DR   HOGENOM; Q4JVN6; -.
DR   OMA; Q4JVN6; RYISTRT.
DR   BioCyc; CJEI306537:JK0957-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    290       Undecaprenyl-diphosphatase 2.
FT                                /FTId=PRO_0000227616.
FT   TRANSMEM    104    124       Potential.
FT   TRANSMEM    128    148       Potential.
FT   TRANSMEM    174    194       Potential.
FT   TRANSMEM    205    225       Potential.
FT   TRANSMEM    237    257       Potential.
FT   TRANSMEM    268    288       Potential.
SQ   SEQUENCE   290 AA;  31766 MW;  7DEAAFF7CCAE65DD CRC64;
     MTTDMTWAQT IILSLIQGLT EFLPVSSSGH LRIFSTLLWG EDAGASFTAV IQLGTELAVL
     VFFAKDIWNI ASAWCKGVWE WLTDLTGKHG RRVHRQSFDY RMGWMVIVGT LPVAVLGYLG
     KDLIRDNLRN LWITATMLVL FSFVFILAER MGRRERSFDE LTMRDSVIMG FAQCLALIPG
     VSRSGGTVSA GLFLNLDREV ATRYSFLLAI PAVLASGLFS LPDAFSPDAG QAASGAQLFV
     GTAIAFAVGY ASIAWLLKFV ANHSFAWFAL WRIPLGLAVM GLLAFGVLQA
//