UPPP3_BACCZ
ID UPPP3_BACCZ Reviewed; 254 AA.
AC Q63DZ3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Undecaprenyl-diphosphatase 3 {ECO:0000255|HAMAP-Rule:MF_01006};
DE EC=3.6.1.27 {ECO:0000255|HAMAP-Rule:MF_01006};
DE AltName: Full=Bacitracin resistance protein 3 {ECO:0000255|HAMAP-Rule:MF_01006};
DE AltName: Full=Undecaprenyl pyrophosphate phosphatase 3 {ECO:0000255|HAMAP-Rule:MF_01006};
GN Name=uppP3 {ECO:0000255|HAMAP-Rule:MF_01006}; Synonyms=bacA3;
GN OrderedLocusNames=BCE33L1270;
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
CC -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate
CC (UPP). Confers resistance to bacitracin. {ECO:0000255|HAMAP-
CC Rule:MF_01006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-
CC trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate;
CC Xref=Rhea:RHEA:28094, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58405, ChEBI:CHEBI:60392; EC=3.6.1.27;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01006};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01006};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01006}.
CC -!- MISCELLANEOUS: Bacitracin is thought to be involved in the inhibition
CC of peptidoglycan synthesis by sequestering undecaprenyl diphosphate,
CC thereby reducing the pool of lipid carrier available.
CC -!- SIMILARITY: Belongs to the UppP family. {ECO:0000255|HAMAP-
CC Rule:MF_01006}.
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DR EMBL; CP000001; AAU18978.1; -; Genomic_DNA.
DR AlphaFoldDB; Q63DZ3; -.
DR SMR; Q63DZ3; -.
DR EnsemblBacteria; AAU18978; AAU18978; BCE33L1270.
DR KEGG; bcz:BCE33L1270; -.
DR OMA; YWKKIKD; -.
DR Proteomes; UP000002612; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; 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-UniRule.
DR HAMAP; MF_01006; Undec_diphosphatase; 1.
DR InterPro; IPR003824; UppP.
DR PANTHER; PTHR30622; PTHR30622; 1.
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; Hydrolase; Membrane;
KW Peptidoglycan synthesis; Transmembrane; Transmembrane helix.
FT CHAIN 1..254
FT /note="Undecaprenyl-diphosphatase 3"
FT /id="PRO_0000151096"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ SEQUENCE 254 AA; 27350 MW; 9C71CC091AF28D5A CRC64;
MGAVEGLTEF LPVSSTGHMI LTGHLIGFDD DRAKVFEVVI QLGSILAVVV IFWKRLWSLV
GIGKVTDGPS LNLLHIIIGM IPAGVLGVLF HSAIKEVLFG PGPVVISLVA GGILMIVAEK
FSKPSTARTL DEITYKQAFT IGMFQCLALW PGFSRSGSTI SGGLLARVSH TAAAEYTFIL
AVPMMVAASG LDLIKSWDIL STADIPLFAT GFITAFVVAM LAIVSFLKLL SRVKLTPFAY
YRFILAAVFY FFIM
