UPPP2_BACHK
ID UPPP2_BACHK Reviewed; 270 AA.
AC Q6HND2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Undecaprenyl-diphosphatase 2 {ECO:0000255|HAMAP-Rule:MF_01006};
DE EC=3.6.1.27 {ECO:0000255|HAMAP-Rule:MF_01006};
DE AltName: Full=Bacitracin resistance protein 2 {ECO:0000255|HAMAP-Rule:MF_01006};
DE AltName: Full=Undecaprenyl pyrophosphate phosphatase 2 {ECO:0000255|HAMAP-Rule:MF_01006};
GN Name=uppP2 {ECO:0000255|HAMAP-Rule:MF_01006}; Synonyms=bacA;
GN OrderedLocusNames=BT9727_0593;
OS Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=281309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=97-27;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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; AE017355; AAT62448.1; -; Genomic_DNA.
DR RefSeq; WP_000434782.1; NC_005957.1.
DR RefSeq; YP_034939.1; NC_005957.1.
DR AlphaFoldDB; Q6HND2; -.
DR SMR; Q6HND2; -.
DR EnsemblBacteria; AAT62448; AAT62448; BT9727_0593.
DR GeneID; 59156460; -.
DR GeneID; 64203818; -.
DR KEGG; btk:BT9727_0593; -.
DR PATRIC; fig|281309.8.peg.624; -.
DR HOGENOM; CLU_060296_1_2_9; -.
DR OMA; VGGRWAQ; -.
DR Proteomes; UP000001301; 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; Transmembrane; Transmembrane helix.
FT CHAIN 1..270
FT /note="Undecaprenyl-diphosphatase 2"
FT /id="PRO_0000151102"
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; 29976 MW; A7A6AA4C7262FCDC CRC64;
MEQFYYILKY LILGLFQGLT EPIPISSSGH LVLAQHLLGL KIEGFSFELL VNSASLLAVL
LIYRNDLIRL TKNGLSYIFT RAEDAKSDFF FIIYLVIATI PAGVIGVLFK DYIDQYLKGV
KMVGISLLIT AVGLWIIRNL RGRKNDGDLS MKDAIIVGLA QACALIPGIS RSGATIVAAM
LLGMKQETAL RFSFLLYIPV SLGGLLLSIT DIAKDPNLDT LFVPYIVAFI ATFIMTYISL
KWFMNIMAKG NLKYFSFYCI IVGVLTLIFL
