ID   UPPP_CORST              Reviewed;         281 AA.
AC   Q9FB58;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Undecaprenyl-diphosphatase;
DE            EC=3.6.1.27;
DE   AltName: Full=Bacitracin resistance protein;
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase;
GN   Name=uppP; Synonyms=bacA, upk;
OS   Corynebacterium striatum.
OG   Plasmid pTP10.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=43770;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M82B;
RX   PubMed=10732668; DOI=10.1007/pl00008668;
RA   Tauch A., Krieft S., Kalinowski J., Puehler A.;
RT   "The 51,409-bp R-plasmid pTP10 from the multiresistant clinical isolate
RT   Corynebacterium striatum M82B is composed of DNA segments initially
RT   identified in soil bacteria and in plant, animal, and human pathogens.";
RL   Mol. Gen. Genet. 263:1-11(2000).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate
CC       (UPP). Confers resistance to bacitracin (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
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:0000305}.
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DR   EMBL; AF024666; AAG03365.1; -; Genomic_DNA.
DR   RefSeq; NP_862231.1; NC_004939.1.
DR   RefSeq; WP_011116972.1; NC_004939.1.
DR   AlphaFoldDB; Q9FB58; -.
DR   SMR; Q9FB58; -.
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 membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW   Peptidoglycan synthesis; Plasmid; Transmembrane; Transmembrane helix.
FT   CHAIN           1..281
FT                   /note="Undecaprenyl-diphosphatase"
FT                   /id="PRO_0000151141"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   281 AA;  30512 MW;  F82700075DB27EA9 CRC64;
     MSFAMTDPAT TMSWVQVIVL SIVQGLTEFL PVSSSGHLRI VSQLFWGEDA GASFTAVIQL
     GTELAVLVFF AKDIWRILTA WFAGLADKSK RNFDYRMGWM VIAGTIPVGL AGVLLKDLIR
     ENFRNLWITA TVLILFSLVF ILAERRGKKT RGFEELTMKD AVVMGLWQCL ALIPGVSRSG
     GTISGGLFLN LDREVATRFS FLLAIPAVLA SGLFSLPDAF DPQAGQAASG LQLLVGSGIG
     FVVGYISIAW LLKFVSNHSF AWFAAYRIPL GLLVMALLGL A