UPPP_CYTH3
ID UPPP_CYTH3 Reviewed; 263 AA.
AC Q11WJ0;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
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;
GN OrderedLocusNames=CHU_0949;
OS Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC
OS 15051 / NCIMB 9469 / D465).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC Cytophaga.
OX NCBI_TaxID=269798;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465;
RX PubMed=17400776; DOI=10.1128/aem.00225-07;
RA Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P.,
RA Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R.,
RA Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B.,
RA McBride M.J.;
RT "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT hutchinsonii.";
RL Appl. Environ. Microbiol. 73:3536-3546(2007).
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; CP000383; ABG58226.1; -; Genomic_DNA.
DR RefSeq; WP_011584341.1; NZ_FPJX01000005.1.
DR AlphaFoldDB; Q11WJ0; -.
DR SMR; Q11WJ0; -.
DR STRING; 269798.CHU_0949; -.
DR EnsemblBacteria; ABG58226; ABG58226; CHU_0949.
DR KEGG; chu:CHU_0949; -.
DR eggNOG; COG1968; Bacteria.
DR HOGENOM; CLU_060296_2_0_10; -.
DR OMA; IEGPFRD; -.
DR OrthoDB; 1826154at2; -.
DR Proteomes; UP000001822; 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..263
FT /note="Undecaprenyl-diphosphatase"
FT /id="PRO_0000290704"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 69..89
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 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ SEQUENCE 263 AA; 29183 MW; DA643E5CE23E3C26 CRC64;
MTWLESIILA IVEGVTEFLP VSSTGHMIIT SALMGIKSDP FTKVFEVAIQ FGAILSVVVL
YFKRFFKSCD FYFKLFVAFI PTAIVGLLLK KHIDTWLENV WVVASTLLVG GIVLLFVDKW
FQKNETEGEE EVSYQTGFLI GCFQCLAMIP GVSRSAATII GGLTQKLTRK AAAEFSFFLA
VPTMFAATAK SLYDEKELIL ESTDKIPLLL LGNVVAFIVA MLAIKFFINI LTKYGFKAFG
YYRIALGALL LILLAMHVDL QVV