YISP_BACSU
ID YISP_BACSU Reviewed; 267 AA.
AC O06728; Q796Q9; Q798I6;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Farnesyl diphosphate phosphatase YisP {ECO:0000305};
DE EC=3.1.7.6 {ECO:0000269|PubMed:25308276};
GN Name=yisP; Synonyms=yucD; OrderedLocusNames=BSU10810;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353932; DOI=10.1099/00221287-143-10-3309;
RA Roche B., Autret S., Levine A., Vannier F., Medina N., Seror S.J.;
RT "A Bacillus subtilis chromosome segment at the 100 degrees to 102 degrees
RT position encoding 11 membrane proteins.";
RL Microbiology 143:3309-3312(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Oudega B., Koningstein G., Duesterhoeft A.;
RT "Bacillus subtilis genome project, DNA sequence from yucA to yucH.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=20713508; DOI=10.1101/gad.1945010;
RA Lopez D., Kolter R.;
RT "Functional microdomains in bacterial membranes.";
RL Genes Dev. 24:1893-1902(2010).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
RN [6] {ECO:0007744|PDB:3WE9}
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 47-ALA-ALA-48; ALA-47;
RP ASP-51; ASP-160 AND ASP-164.
RC STRAIN=168;
RX PubMed=25308276; DOI=10.1016/j.chembiol.2014.08.018;
RA Feng X., Hu Y., Zheng Y., Zhu W., Li K., Huang C.H., Ko T.P., Ren F.,
RA Chan H.C., Nega M., Bogue S., Lopez D., Kolter R., Goetz F., Guo R.T.,
RA Oldfield E.;
RT "Structural and functional analysis of Bacillus subtilis YisP reveals a
RT role of its product in biofilm production.";
RL Chem. Biol. 21:1557-1563(2014).
CC -!- FUNCTION: A farnesyl diphosphate (FPP) phosphatase. Involved in biofilm
CC formation, its disruption blocks biofilm synthesis which is restored by
CC exogenous farnesol (PubMed:25308276). Releases diphosphate from FPP,
CC was initally suggested to be a squalene synthase. Diphosphate release
CC is higher from FPP than geranyl pyrophosphate (GPP) or geranylgeranyl
CC pyrophosphate (GGPP). Biofilm synthesis is partially restored by
CC exogenous squalene, beta-carotene or retinol. Required for integrity of
CC cell membrane lipid rafts (PubMed:20713508). Involved in spatial
CC organization of membranes, required for the flotillin-like proteins
CC FloT and FloA to function correctly (PubMed:23651456).
CC {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:23651456,
CC ECO:0000269|PubMed:25308276}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-farnesol +
CC diphosphate; Xref=Rhea:RHEA:27526, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16619, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=3.1.7.6;
CC Evidence={ECO:0000269|PubMed:25308276};
CC -!- ACTIVITY REGULATION: Diphosphate release from FPP is inhibited by
CC zaragozic acid. {ECO:0000269|PubMed:20713508}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.47 uM for farnesyl pyrophosphate {ECO:0000269|PubMed:20713508};
CC KM=14.9 uM for geranyl pyrophosphate {ECO:0000269|PubMed:20713508};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25308276}.
CC -!- DISRUPTION PHENOTYPE: Loss of biofilm formation (PubMed:20713508,
CC PubMed:25308276). Loss of a dark-orange pigment from cells, alteration
CC of cellular lipid profile. Significant reduction of proteins found in
CC detergent-resistant membrane (DRM) fractions (PubMed:20713508).
CC Decrease in membrane fluidity, about 30% decrease in protein secretion
CC (PubMed:23651456). {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:25308276}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a squalene synthase
CC (PubMed:20713508). Further characterization suggests it is actually a
CC farnesyl diphosphate phosphatase (PubMed:25308276).
CC {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:25308276}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA70644.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB12920.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y09476; CAA70644.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z93940; CAB07958.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12920.1; ALT_INIT; Genomic_DNA.
DR PIR; G69837; G69837.
DR RefSeq; NP_388961.1; NC_000964.3.
DR RefSeq; WP_010886471.1; NZ_JNCM01000035.1.
DR PDB; 3WE9; X-ray; 1.92 A; A=1-267.
DR PDBsum; 3WE9; -.
DR AlphaFoldDB; O06728; -.
DR SMR; O06728; -.
DR STRING; 224308.BSU10810; -.
DR PaxDb; O06728; -.
DR PRIDE; O06728; -.
DR DNASU; 936353; -.
DR EnsemblBacteria; CAB12920; CAB12920; BSU_10810.
DR GeneID; 936353; -.
DR KEGG; bsu:BSU10810; -.
DR PATRIC; fig|224308.179.peg.1162; -.
DR eggNOG; COG1562; Bacteria.
DR InParanoid; O06728; -.
DR BioCyc; BSUB:BSU10810-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR002060; Squ/phyt_synthse.
DR Pfam; PF00494; SQS_PSY; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..267
FT /note="Farnesyl diphosphate phosphatase YisP"
FT /id="PRO_0000388332"
FT MUTAGEN 47..48
FT /note="AA->DD: Greater than wild-type diphosphate release."
FT /evidence="ECO:0000269|PubMed:25308276"
FT MUTAGEN 47
FT /note="A->D: Wild-type diphosphate release."
FT /evidence="ECO:0000269|PubMed:25308276"
FT MUTAGEN 51
FT /note="D->A: Loss of diphosphate release."
FT /evidence="ECO:0000269|PubMed:25308276"
FT MUTAGEN 160
FT /note="D->A: Loss of diphosphate release."
FT /evidence="ECO:0000269|PubMed:25308276"
FT MUTAGEN 164
FT /note="D->A: Loss of diphosphate release."
FT /evidence="ECO:0000269|PubMed:25308276"
FT HELIX 1..18
FT /evidence="ECO:0007829|PDB:3WE9"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:3WE9"
FT HELIX 31..47
FT /evidence="ECO:0007829|PDB:3WE9"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:3WE9"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:3WE9"
FT HELIX 111..133
FT /evidence="ECO:0007829|PDB:3WE9"
FT HELIX 138..158
FT /evidence="ECO:0007829|PDB:3WE9"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:3WE9"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:3WE9"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:3WE9"
FT HELIX 192..214
FT /evidence="ECO:0007829|PDB:3WE9"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3WE9"
FT HELIX 221..243
FT /evidence="ECO:0007829|PDB:3WE9"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:3WE9"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3WE9"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:3WE9"
SQ SEQUENCE 267 AA; 30621 MW; 93932E09E77C72AA CRC64;
MKEIKEAYQQ CGQIVGEYAP ACFKALSYLP LKQRQASWAV LSFCHTAASA DEKVLPAFEA
KADHVYQRTN NGKQHLWKAF DHAYRTFTLE SEPFREFIAA QKEDAKPYDD LDELLMYAYR
TGGAAGLMLL PILTRRKQDQ LKQAAVSLGL AIQLVRFLSD LGTDQQKNRI PRQVMQQFGY
TEADLQKGTV NKAFTMTWEY IAFEAEAYLE ECQDALPLFP QYSQKTVKAA LHLHRAVLEK
IRAKQHDVFQ YHFALTETEV KQILSDI
