(data stored in ACNUC7421 zone)

HOGENOM: CEALG1_1_PE1001

ID   CEALG1_1_PE1001                      STANDARD;      PRT;   264 AA.
AC   CEALG1_1_PE1001; E6X552;
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; EC=3.6.1 27;AltName:
DE   Full=Bacitracin resistance protein;AltName: Full=Undecaprenyl
DE   pyrophosphate phosphatase; (CEALG1_1.PE1001).
GN   Name=uppP; OrderedLocusNames=Celal_1038;
OS   CELLULOPHAGA ALGICOLA DSM 14237.
OC   Bacteria; Bacteroidetes; Flavobacteria; Flavobacteriales;
OC   Flavobacteriaceae; Cellulophaga.
OX   NCBI_TaxID=688270;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CEALG1_1.PE1001.
CC       Cellulophaga algicola DSM 14237 chromosome, complete genome.
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:E6X552_CELAD
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 inner membrane; Multi-pass membrane
CC       protein (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; E6X552; -.
DR   EMBL; CP002453; ADV48363.1; -; Genomic_DNA.
DR   RefSeq; YP_004163861.1; NC_014934.1.
DR   GeneID; 10143425; -.
DR   GenomeReviews; CP002453_GR; Celal_1038.
DR   KEGG; cao:Celal_1038; -.
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: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   HOGENOMDNA; CEALG1_1.PE1001; -.
KW   undecaprenyl-diphosphatase;
KW   Antibiotic resistance; Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Hydrolase;
KW   Membrane; Peptidoglycan synthesis; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   264 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MEVIDAIILG IIQGLTEFLP VSSSGHLELG KAILGDHSVP EESLLFTVVL HFATALSTLV
     VFRKDVWELL CGLFQFKWNE ETQFSIKIII SMLPAVFVGL FFEKQLESFF GGNVRFVGFM
     LLVTAVLLYL ADKAKDTDKK VSFKSAFLVG ISQAIAMLPG ISRSGATIST SVLLGVDKTK
     AARFSFLMVV PLIFGKIFKD LLGGELTFDG DNNVAMGAGF IAAFIAGLGA CTWMIQLVKK
     SKLSYFAIYC LIVGLIAIAY GYLA
//

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