ID   BCRC_BACSU              Reviewed;         193 AA.
AC   P94571;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Undecaprenyl-diphosphatase BcrC;
DE            EC=3.6.1.27;
DE   AltName: Full=Undecaprenyl pyrophosphate phosphatase;
GN   Name=bcrC; Synonyms=ywoA; OrderedLocusNames=BSU36530;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA   Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA   Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA   Kunst F., Danchin A., Glaser P.;
RT   "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT   degrees).";
RL   Microbiology 143:3313-3328(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION IN BACITRACIN RESISTANCE, AND INDUCTION.
RC   STRAIN=168 / CU1065;
RX   PubMed=12399481; DOI=10.1128/jb.184.22.6123-6129.2002;
RA   Cao M., Helmann J.D.;
RT   "Regulation of the Bacillus subtilis bcrC bacitracin resistance gene by two
RT   extracytoplasmic function sigma factors.";
RL   J. Bacteriol. 184:6123-6129(2002).
RN   [4]
RP   FUNCTION.
RC   STRAIN=168;
RX   PubMed=14612242; DOI=10.1016/s0378-1097(03)00738-9;
RA   Bernard R., Joseph P., Guiseppi A., Chippaux M., Denizot F.;
RT   "YtsCD and YwoA, two independent systems that confer bacitracin resistance
RT   to Bacillus subtilis.";
RL   FEMS Microbiol. Lett. 228:93-97(2003).
RN   [5]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=12486040; DOI=10.1128/jb.185.1.51-59.2003;
RA   Ohki R., Tateno K., Okada Y., Okajima H., Asai K., Sadaie Y., Murata M.,
RA   Aiso T.;
RT   "A bacitracin-resistant Bacillus subtilis gene encodes a homologue of the
RT   membrane-spanning subunit of the Bacillus licheniformis ABC transporter.";
RL   J. Bacteriol. 185:51-59(2003).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=15946938; DOI=10.1074/jbc.m413750200;
RA   Bernard R., El Ghachi M., Mengin-Lecreulx D., Chippaux M., Denizot F.;
RT   "BcrC from Bacillus subtilis acts as an undecaprenyl pyrophosphate
RT   phosphatase in bacitracin resistance.";
RL   J. Biol. Chem. 280:28852-28857(2005).
RN   [7]
RP   INDUCTION.
RC   STRAIN=168 / 1604;
RX   PubMed=17434969; DOI=10.1128/jb.00130-07;
RA   Jervis A.J., Thackray P.D., Houston C.W., Horsburgh M.J., Moir A.;
RT   "SigM-responsive genes of Bacillus subtilis and their promoters.";
RL   J. Bacteriol. 189:4534-4538(2007).
RN   [8]
RP   INDUCTION.
RC   STRAIN=168;
RX   PubMed=18156261; DOI=10.1128/jb.01497-07;
RA   Tseng C.-L., Shaw G.-C.;
RT   "Genetic evidence for the actin homolog gene mreBH and the bacitracin
RT   resistance gene bcrC as targets of the alternative sigma factor sigI of
RT   Bacillus subtilis.";
RL   J. Bacteriol. 190:1561-1567(2008).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate
CC       (UPP). Confers resistance to bacitracin. {ECO:0000269|PubMed:12399481,
CC       ECO:0000269|PubMed:14612242, ECO:0000269|PubMed:15946938}.
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:0000269|PubMed:15946938};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15946938};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:15946938}.
CC   -!- INDUCTION: Expression is sigma M, sigma X and sigma I-dependent.
CC       Induced by vancomycin and bacitracin, via sigma M. Expression is
CC       maximal during early exponential phase and decreases during stationary
CC       phase. {ECO:0000269|PubMed:12399481, ECO:0000269|PubMed:12486040,
CC       ECO:0000269|PubMed:17434969, ECO:0000269|PubMed:18156261}.
CC   -!- DISRUPTION PHENOTYPE: Disruption results in a marked decrease of
CC       resistance to bacitracin. {ECO:0000269|PubMed:12486040}.
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 BcrC/YbjG family. {ECO:0000305}.
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DR   EMBL; Z82987; CAB05382.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15670.1; -; Genomic_DNA.
DR   PIR; D70064; D70064.
DR   RefSeq; NP_391534.1; NC_000964.3.
DR   RefSeq; WP_003243362.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P94571; -.
DR   SMR; P94571; -.
DR   STRING; 224308.BSU36530; -.
DR   TCDB; 9.B.105.1.3; the lead resistance fusion protein (pbrbc) family.
DR   PaxDb; 224308-BSU36530; -.
DR   EnsemblBacteria; CAB15670; CAB15670; BSU_36530.
DR   GeneID; 936946; -.
DR   KEGG; bsu:BSU36530; -.
DR   PATRIC; fig|224308.179.peg.3953; -.
DR   eggNOG; COG0671; Bacteria.
DR   InParanoid; P94571; -.
DR   OrthoDB; 9789113at2; -.
DR   PhylomeDB; P94571; -.
DR   BioCyc; BSUB:BSU36530-MONOMER; -.
DR   BRENDA; 3.6.1.27; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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-KW.
DR   CDD; cd03385; PAP2_BcrC_like; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   InterPro; IPR033879; UPP_Pase.
DR   PANTHER; PTHR14969; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1.
DR   PANTHER; PTHR14969:SF61; UNDECAPRENYL-DIPHOSPHATASE BCRC; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   1: Evidence at protein level;
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..193
FT                   /note="Undecaprenyl-diphosphatase BcrC"
FT                   /id="PRO_0000049990"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   193 AA;  21723 MW;  E7C1ACC1556BC6CE CRC64;
     MNYEIFKAIH GLSHHNSVLD SIMVFITEYA IVAYALILLA IWLFGNTQSR KHVLYAGITG
     IAGLVINYLI TLVYFEPRPF VAHTVHTLIP HAADASFPSD HTTGALAISI AMLFRNRKIG
     WPLVIFGLLT GFSRIWVGHH YPVDVLGSLV VAIIIGFLFF RFSDLLRPFV DLVVRIYEAI
     INKLTKKPTD QNF
//