ID   UPPP1_BACCR             Reviewed;         270 AA.
AC   Q81HV4;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Undecaprenyl-diphosphatase 1 {ECO:0000255|HAMAP-Rule:MF_01006};
DE            EC=3.6.1.27 {ECO:0000255|HAMAP-Rule:MF_01006};
DE   AltName: Full=Bacitracin resistance protein 1 {ECO:0000255|HAMAP-Rule:MF_01006};
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase 1 {ECO:0000255|HAMAP-Rule:MF_01006};
GN   Name=uppP1 {ECO:0000255|HAMAP-Rule:MF_01006}; Synonyms=bacA1, upk1;
GN   OrderedLocusNames=BC_0677;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(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 membrane {ECO:0000255|HAMAP-Rule:MF_01006};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-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; AE016877; AAP07691.1; -; Genomic_DNA.
DR   RefSeq; NP_830490.1; NC_004722.1.
DR   RefSeq; WP_000434794.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81HV4; -.
DR   SMR; Q81HV4; -.
DR   STRING; 226900.BC_0677; -.
DR   EnsemblBacteria; AAP07691; AAP07691; BC_0677.
DR   GeneID; 67505373; -.
DR   KEGG; bce:BC0677; -.
DR   PATRIC; fig|226900.8.peg.637; -.
DR   HOGENOM; CLU_060296_1_2_9; -.
DR   OMA; VGGRWAQ; -.
DR   Proteomes; UP000001417; 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 membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW   Peptidoglycan synthesis; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..270
FT                   /note="Undecaprenyl-diphosphatase 1"
FT                   /id="PRO_0000151091"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01006"
SQ   SEQUENCE   270 AA;  29934 MW;  304CAA47A19A5E4B CRC64;
     MEQFYYVLKY LILGLFQGLT EPIPISSSGH LVLAQHLLGL KIEGFSFELL VNSASLLAVL
     LIYRNDLIRL TKNGLSYIFT RAEDAKSDFF FIIYLVIATI PAGVIGVLFK DYIDQYLKGV
     KMVGISLLIT AVGLWIIRNL RGRKNDGDLS MKDAIIVGLA QACALIPGIS RSGATIVAAM
     LLGMKQETAL RFSFLLYIPV SLGGLLLSIT DIANDPNLDT LFVPYVVAFI ATFIMTYISL
     KWFMNIMAKG NLKYFSFYCI IVGVLTLIFL