(data stored in ACNUC7421 zone)

HOGENOM: FRASN_1_PE100

ID   FRASN_1_PE100                        STANDARD;      PRT;   278 AA.
AC   FRASN_1_PE100; A8LBA8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Undecaprenyl-diphosphatase 1; EC=3.6.1 27;AltName:
DE   Full=Bacitracin resistance protein 1;AltName: Full=Undecaprenyl
DE   pyrophosphate phosphatase 1; (FRASN_1.PE100).
GN   Name=uppP1; OrderedLocusNames=Franean1_0102;
OS   FRANKIA SP. EAN1PEC.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Frankineae;
OC   Frankiaceae; Frankia.
OX   NCBI_TaxID=298653;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS FRASN_1.PE100.
CC       Frankia sp. EAN1pec, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:A8LBA8_FRASN
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       (By similarity).
CC   -!- SIMILARITY: Belongs to the UppP family.
CC   -!- GENE_FAMILY: HOG000218357 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A8LBA8; -.
DR   EMBL; CP000820; ABW09569.1; -; Genomic_DNA.
DR   RefSeq; YP_001504475.1; NC_009921.1.
DR   STRING; A8LBA8; -.
DR   GeneID; 5668527; -.
DR   GenomeReviews; CP000820_GR; Franean1_0102.
DR   KEGG; fre:Franean1_0102; -.
DR   OMA; DWLIGLI; -.
DR   ProtClustDB; PRK00281; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:HAMAP.
DR   GO; GO:0007047; P:cellular 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; Undec_diphosphatase; 1; -.
DR   InterPro; IPR003824; Bacitracin-R_BacA.
DR   Pfam; PF02673; BacA; 1.
DR   TIGRFAMs; TIGR00753; Undec_PP_bacA; 1.
DR   HOGENOMDNA; FRASN_1.PE100; -.
KW   undecaprenyl pyrophosphate phosphatase;
KW   Antibiotic resistance; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Hydrolase;
KW   Kinase; Membrane; Peptidoglycan synthesis; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   278 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNIVEAVFLG AVEGLTEFLP VSSTGHLTII EKLLGYSIDD PDITAFTAII QVGAVFATLL
     YLRHDFRRII AALARGVTRP EYRDHPDFRF GVAVIVGSIP IGIVGLLFKD QIETTLRSLW
     FVGTALIGWS AVMGYADRVA TQKRHEDDVT WKDTLVIGVV QCMALIPGIS RSGSTMSAGL
     LRGIDRVTVT RLSFFLSIPA LFAAALLQVV TESSNIEQGV GWTVTITATV VSFVTAYFAI
     AWLLKFVARH SYSVFIYYRL ALGSVILFLL ATGIISAT
//

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