ID   UPPP_HALOH              Reviewed;         259 AA.
AC   B8CWG2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
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=Hore_08750;
OS   Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae;
OC   Halothermothrix.
OX   NCBI_TaxID=373903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 168 / OCM 544 / DSM 9562;
RX   PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA   Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA   Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT   "Genome analysis of the anaerobic thermohalophilic bacterium
RT   Halothermothrix orenii.";
RL   PLoS ONE 4:E4192-E4192(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; CP001098; ACL69631.1; -; Genomic_DNA.
DR   RefSeq; WP_012635818.1; NC_011899.1.
DR   AlphaFoldDB; B8CWG2; -.
DR   SMR; B8CWG2; -.
DR   STRING; 373903.Hore_08750; -.
DR   KEGG; hor:Hore_08750; -.
DR   eggNOG; COG1968; Bacteria.
DR   HOGENOM; CLU_060296_1_2_9; -.
DR   OrthoDB; 9808289at2; -.
DR   Proteomes; UP000000719; Chromosome.
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   NCBIfam; TIGR00753; undec_PP_bacA; 1.
DR   PANTHER; PTHR30622; UNDECAPRENYL-DIPHOSPHATASE; 1.
DR   PANTHER; PTHR30622:SF4; UNDECAPRENYL-DIPHOSPHATASE; 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..259
FT                   /note="Undecaprenyl-diphosphatase"
FT                   /id="PRO_1000148816"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        75..95
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        179..199
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        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ   SEQUENCE   259 AA;  28837 MW;  99088AE5C50CD683 CRC64;
     MEIFKVIFLG IIQGLTEFLP ISSSGHLVLF QELLGINTDQ ITLDVFLHFG TVIPVLIIFW
     DDVRDIIFFK KEKRWLTILI LVGIIPTGII GILFEDFFAN LFSSVKTVGF MLLVTGFLLY
     LSEKLSNYNK ELKEMQYHNA LIVGVAQGMA IIPGISRSGS TIVASLLQGF DRDAAARYSF
     LLSAPVIFGA GLVELKDALS TGLEQLTWLS IIIGTIFAAL SGYFAIKYLL YILRKGKLTV
     FAYYCWIVGI MIIILAGIF
//