SQHC_BACSU
ID SQHC_BACSU Reviewed; 632 AA.
AC Q796C3; O34650;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Sporulenol synthase;
DE EC=4.2.1.137;
DE AltName: Full=Tetraprenyl-beta-curcumene cyclase;
GN Name=sqhC; OrderedLocusNames=BSU19320;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT terC and odhAB loci cloned in a yeast artificial chromosome.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
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 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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21627333; DOI=10.1021/ja203779h;
RA Sato T., Yoshida S., Hoshino H., Tanno M., Nakajima M., Hoshino T.;
RT "Sesquarterpenes (C35 terpenes) biosynthesized via the cyclization of a
RT linear C35 isoprenoid by a tetraprenyl-beta-curcumene synthase and a
RT tetraprenyl-beta-curcumene cyclase: identification of a new terpene
RT cyclase.";
RL J. Am. Chem. Soc. 133:9734-9737(2011).
CC -!- FUNCTION: Catalyzes the cyclization of tetraprenyl beta-curcumene into
CC sporulenol. {ECO:0000269|PubMed:21627333}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sporulenol = (R)-tetraprenyl-beta-curcumene + H2O;
CC Xref=Rhea:RHEA:34255, ChEBI:CHEBI:15377, ChEBI:CHEBI:64801,
CC ChEBI:CHEBI:67182; EC=4.2.1.137;
CC Evidence={ECO:0000269|PubMed:21627333};
CC -!- PATHWAY: Secondary metabolite biosynthesis; hopanoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No effect on biofilm formation.
CC {ECO:0000269|PubMed:20713508}.
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB84441.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF027868; AAB84441.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB13824.2; -; Genomic_DNA.
DR PIR; A69718; A69718.
DR RefSeq; NP_389814.2; NC_000964.3.
DR RefSeq; WP_004399534.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; Q796C3; -.
DR SMR; Q796C3; -.
DR STRING; 224308.BSU19320; -.
DR PaxDb; Q796C3; -.
DR EnsemblBacteria; CAB13824; CAB13824; BSU_19320.
DR GeneID; 939443; -.
DR KEGG; bsu:BSU19320; -.
DR PATRIC; fig|224308.179.peg.2113; -.
DR eggNOG; COG1657; Bacteria.
DR InParanoid; Q796C3; -.
DR OMA; CWARQTI; -.
DR PhylomeDB; Q796C3; -.
DR BioCyc; BSUB:BSU19320-MON; -.
DR BRENDA; 4.2.1.137; 658.
DR UniPathway; UPA00337; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016866; F:intramolecular transferase activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016104; P:triterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd02892; SQCY_1; 1.
DR InterPro; IPR032696; SQ_cyclase_C.
DR InterPro; IPR032697; SQ_cyclase_N.
DR InterPro; IPR018333; Squalene_cyclase.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11764; PTHR11764; 1.
DR Pfam; PF13243; SQHop_cyclase_C; 1.
DR Pfam; PF13249; SQHop_cyclase_N; 1.
DR SFLD; SFLDG01016; Prenyltransferase_Like_2; 1.
DR SUPFAM; SSF48239; SSF48239; 2.
DR TIGRFAMs; TIGR01787; squalene_cyclas; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lyase; Membrane; Reference proteome; Repeat.
FT CHAIN 1..632
FT /note="Sporulenol synthase"
FT /id="PRO_0000360070"
FT REPEAT 395..436
FT /note="PFTB 1"
FT REPEAT 465..505
FT /note="PFTB 2"
FT REPEAT 513..554
FT /note="PFTB 3"
FT ACT_SITE 377
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
SQ SEQUENCE 632 AA; 71224 MW; C79E4090386832F6 CRC64;
MGTLQEKVRR FQKKTITELR DRQNADGSWT FCFEGPIMTN SFFILLLTSL DEGENEKELI
SSLAAGIHAK QQPDGTFINY PDETRGNLTA TVQGYVGMLA SGCFHRTEPH MKKAEQFIIS
HGGLRHVHFM TKWMLAANGL YPWPALYLPL SLMALPPTLP IHFYQFSSYA RIHFAPMAVT
LNQRFVLINR NISSLHHLDP HMTKNPFTWL RSDAFEERDL TSILLHWKRV FHAPFAFQQL
GLQTAKTYML DRIEKDGTLY SYASATIYMV YSLLSLGVSR YSPIIRRAIT GIKSLVTKCN
GIPYLENSTS TVWDTALISY ALQKNGVTET DGSVTKAADF LLERQHTKIA DWSVKNPNSV
PGGWGFSNIN TNNPDCDDTT AVLKAIPRNH SPAAWERGVS WLLSMQNNDG GFSAFEKNVN
HPLIRLLPLE SAEDAAVDPS TADLTGRVLH FLGEKVGFTE KHQHIQRAVK WLFEHQEQNG
SWYGRWGVCY IYGTWAALTG MHACGVDRKH PGIQKALRWL KSIQNDDGSW GESCKSAEIK
TYVPLHRGTI VQTAWALDAL LTYENSEHPS VVKGMQYLTD SSSHSADSLA YPAGIGLPKQ
FYIRYHSYPY VFSLLAVGKY LDSIEKETAN ET
