(data stored in ACNUC7421 zone)

HOGENOM: AZOS1_1_PE101

ID   AZOS1_1_PE101                        STANDARD;      PRT;   266 AA.
AC   AZOS1_1_PE101; D3NQR0;
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; (AZOS1_1.PE101).
GN   Name=bacA; Synonyms=uppP; OrderedLocusNames=AZL_001010;
OS   AZOSPIRILLUM SP. B510.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=137722;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AZOS1_1.PE101.
CC       Azospirillum sp. B510 chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:D3NQR0_AZOS1
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: HOG000218356 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D3NQR0; -.
DR   EMBL; AP010946; BAI70739.1; -; Genomic_DNA.
DR   RefSeq; YP_003447283.1; NC_013854.1.
DR   GeneID; 8790916; -.
DR   GenomeReviews; AP010946_GR; AZL_001010.
DR   KEGG; azl:AZL_001010; -.
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   TIGRFAMs; TIGR00753; Undec_PP_bacA; 1.
DR   HOGENOMDNA; AZOS1_1.PE101; -.
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   266 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MMIDQYLDAT LLGLIEGLTE FLPVSSTGHL IMLDELLGFE GPPGKVFEVV IQLGAILAIC
     VVYFQRLWHV ATGLKDDPGA RRFVMAVVIA FLPAMVLGAG LHGIIKAVLF NPTVVSIALI
     VGGIAILLVE RMVPVPRYHR IENFPAPLAL KIGFCQCLAL VPGVSRSGAS ILGALLMGVD
     RKTAAEFSFF LAVPTMAGAT VYDLYKNWSG MSFDSGLLIL VGFVTAFIAA ALVVKTLVDF
     VGRYGFTPFG WYRIAVGTGM LAFLYL
//

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