UPPP_PSEAE
ID UPPP_PSEAE Reviewed; 277 AA.
AC Q9I2E5;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Undecaprenyl-diphosphatase {ECO:0000255|HAMAP-Rule:MF_01006};
DE EC=3.6.1.27 {ECO:0000255|HAMAP-Rule:MF_01006};
DE AltName: Full=Bacitracin resistance protein {ECO:0000255|HAMAP-Rule:MF_01006};
DE AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_01006};
GN Name=uppP {ECO:0000255|HAMAP-Rule:MF_01006}; Synonyms=bacA, upk;
GN OrderedLocusNames=PA1959;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01006}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG05347.1; -; Genomic_DNA.
DR PIR; F83401; F83401.
DR RefSeq; NP_250649.1; NC_002516.2.
DR RefSeq; WP_003113476.1; NZ_QZGE01000030.1.
DR AlphaFoldDB; Q9I2E5; -.
DR SMR; Q9I2E5; -.
DR STRING; 287.DR97_5889; -.
DR PaxDb; Q9I2E5; -.
DR PRIDE; Q9I2E5; -.
DR EnsemblBacteria; AAG05347; AAG05347; PA1959.
DR GeneID; 877690; -.
DR KEGG; pae:PA1959; -.
DR PATRIC; fig|208964.12.peg.2042; -.
DR PseudoCAP; PA1959; -.
DR HOGENOM; CLU_060296_2_0_6; -.
DR InParanoid; Q9I2E5; -.
DR OMA; IEGPFRD; -.
DR PhylomeDB; Q9I2E5; -.
DR BioCyc; PAER208964:G1FZ6-1997-MON; -.
DR Proteomes; UP000002438; 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 inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW Peptidoglycan synthesis; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..277
FT /note="Undecaprenyl-diphosphatase"
FT /id="PRO_0000151181"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ SEQUENCE 277 AA; 30724 MW; 52DBB5917B8583CB CRC64;
MEWWTAFQAF ILGVVEGLTE FLPISSTGHQ IIVADLIGFG GERAKAFNII IQLAAILAVV
WEFRGKIFQV VRDLPSQRQA QRFTANLLIA FFPAVVLGVL FADLIHEWLF NPITVALALV
VGGVVMLWAE RRKHVIRAEH VDDMTWKDAL KIGCAQCLAM IPGTSRSGAT IIGGLLFGLS
RKAATEFSFF LAMPTMVGAA VYSGYVYRDL FRPEDLPVFA VGFVTSFVFA MLAVRALLKF
IGNHSYAAFA WYRIAFGLLI LATWQFHLID WSTAGEV
