(data stored in ACNUC7421 zone)

HOGENOM: SHELP_1_PE1002

ID   SHELP_1_PE1002                       STANDARD;      PRT;   266 AA.
AC   SHELP_1_PE1002; A3QBM7;
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; (SHELP_1.PE1002).
GN   Name=uppP; OrderedLocusNames=Shew_1004;
OS   SHEWANELLA LOIHICA PV-4.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHELP_1.PE1002.
CC       Shewanella loihica PV-4, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:UPPP_SHELP
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   -!- SIMILARITY: Belongs to the UppP family.
CC   -!- GENE_FAMILY: HOG000218357 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A3QBM7; -.
DR   EMBL; CP000606; ABO22875.1; -; Genomic_DNA.
DR   RefSeq; YP_001093134.1; NC_009092.1.
DR   STRING; A3QBM7; -.
DR   GeneID; 4920564; -.
DR   GenomeReviews; CP000606_GR; Shew_1004.
DR   KEGG; slo:Shew_1004; -.
DR   NMPDR; fig|323850.3.peg.2758; -.
DR   eggNOG; COG1968; -.
DR   OMA; FKAWIAS; -.
DR   PhylomeDB; A3QBM7; -.
DR   ProtClustDB; PRK00281; -.
DR   BioCyc; SLOI323850:SHEW_1004-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:EC.
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; SHELP_1.PE1002; -.
KW   undecaprenyl pyrophosphate phosphatase;
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;
     MDIFQVIVLA LIQGLTEFLP ISSSAHLILP AQLLGWQDQG LTFDVAVNTG SLLAVVIYFR
     RELFSMFTAW TSSLVTRQQT QESKLAWWII LATIPAVIFG FTAKDFISTH LRNIEVIATT
     TIVFGLLLWW ADKLNREGFS EFQVGWKKAL LIGFAQAMAL IPGTSRSGAT ITAALALGLS
     REAAARFSFL MSVPVSLGAA ILVVKDLLSS QEAIDYQALV LGTALSFVAA YLCIHYFLKI
     ISRMGMTPFV IYRLALGAIL CVVIFA
//

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