UPPP_ALKEH
ID UPPP_ALKEH Reviewed; 290 AA.
AC Q0AAG2;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
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}; OrderedLocusNames=Mlg_0821;
OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Alkalilimnicola.
OX NCBI_TaxID=187272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000453; ABI56175.1; -; Genomic_DNA.
DR RefSeq; WP_011628570.1; NC_008340.1.
DR AlphaFoldDB; Q0AAG2; -.
DR SMR; Q0AAG2; -.
DR EnsemblBacteria; ABI56175; ABI56175; Mlg_0821.
DR KEGG; aeh:Mlg_0821; -.
DR eggNOG; COG1968; Bacteria.
DR HOGENOM; CLU_060296_1_2_6; -.
DR OMA; WEFLATG; -.
DR OrthoDB; 1826154at2; -.
DR Proteomes; UP000001962; 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..290
FT /note="Undecaprenyl-diphosphatase"
FT /id="PRO_0000290680"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ SEQUENCE 290 AA; 31495 MW; 9A92515DF581D1ED CRC64;
MALWIAALLG VIQGIFMFLP VSSTAHMVLT EHWLIARGET LPPPESAEMI LFALVVHVGT
LVSIAVVFWP SLWRFSLNAL GGAWEWAGRG GRGGLPLYWR LFWLGMFSVL CTGVLGLTLK
ATFEHVFASP LMIAGTLTLT GILLWWTDRL APRRRGLKGI NLKVAGVIGL AQGFALMPGL
SRSAMTIVFA LFTGLKRRWA AEYSFFLAIP TICAATLLQA IEVYRLGLPN TVGFSALAVG
FVVAAIVGII SLKLVIYFLY RARLKVFSFY VWALALGIAT GLIDLAPALG
