UPPP_KORVE
ID UPPP_KORVE Reviewed; 286 AA.
AC Q1IPW7;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
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};
GN OrderedLocusNames=Acid345_2082;
OS Koribacter versatilis (strain Ellin345).
OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC Candidatus Koribacter.
OX NCBI_TaxID=204669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin345;
RX PubMed=19201974; DOI=10.1128/aem.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP000360; ABF41083.1; -; Genomic_DNA.
DR RefSeq; WP_011522884.1; NC_008009.1.
DR AlphaFoldDB; Q1IPW7; -.
DR SMR; Q1IPW7; -.
DR STRING; 204669.Acid345_2082; -.
DR EnsemblBacteria; ABF41083; ABF41083; Acid345_2082.
DR KEGG; aba:Acid345_2082; -.
DR eggNOG; COG1968; Bacteria.
DR HOGENOM; CLU_060296_2_0_0; -.
DR OMA; IEGPFRD; -.
DR OrthoDB; 1826154at2; -.
DR Proteomes; UP000002432; 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.
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..286
FT /note="Undecaprenyl-diphosphatase"
FT /id="PRO_0000290674"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ SEQUENCE 286 AA; 31183 MW; 29948C2DDD70D44B CRC64;
MNAYLLAALL GVVEGLTEFL PVSSTAHLRI CEALLHIDLG DGFWKMFSIV IQLGAILCLP
IYFRARISEF FATFPKGKSG NHTALTHPLT LTIIAFLCTA IPAFLFTKII GKHLESVIIM
GSALLIGGIV MWIVDVMFAD KGATDDMDKM SVGQAIWIGL CQVLSAVFPG TSRSMSTIAA
GQLSGMTRAA ALEFSFFLSI PTMVVATCYD LLKTLRHKDE AGAALGVVHM DAHAWITLAI
GFIVSFIVAY FVVAWFMKWV RTRGFVPFAV YRIVVGIAVL AWALKR
