UPPP_PARMW
ID UPPP_PARMW Reviewed; 287 AA.
AC Q7U482;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=SYNW2189;
OS Parasynechococcus marenigrum (strain WH8102).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Parasynechococcus; Parasynechococcus marenigrum.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(2003).
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}.
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DR EMBL; BX569694; CAE08704.1; -; Genomic_DNA.
DR RefSeq; WP_011129044.1; NC_005070.1.
DR AlphaFoldDB; Q7U482; -.
DR SMR; Q7U482; -.
DR STRING; 84588.SYNW2189; -.
DR EnsemblBacteria; CAE08704; CAE08704; SYNW2189.
DR KEGG; syw:SYNW2189; -.
DR eggNOG; COG1968; Bacteria.
DR HOGENOM; CLU_060296_1_0_3; -.
DR OMA; IEGPFRD; -.
DR OrthoDB; 1826154at2; -.
DR Proteomes; UP000001422; 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; Transmembrane; Transmembrane helix.
FT CHAIN 1..287
FT /note="Undecaprenyl-diphosphatase"
FT /id="PRO_0000151225"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ SEQUENCE 287 AA; 30681 MW; 937390DC6FA3B095 CRC64;
MADPSASLGL WEACWRDLVL GIVQGLTEFL PISSTAHLKV VPVLLDWGDP GVSVTAAIQL
GSIVAVIAYF RRDLAQVMQG ISKAFRHGQW REPEARLGIA MAVGTLPILA VGLAIKLFWD
EGYETSPLRS VPSIAVVSIV MALLLAVAER MGPRRKQLSD VSGRDGLVVG LAQVLALIPG
VSRSGSTLTA SLLDGWQRAD AARFSFLLGI PAITIAGIVE LKDALAATAD AGPLPLVIGI
LAATVVSWLA IDWLLKFLQR HSTWLFVAYR LLFGVGLLAW WSIHGAH