BGS1_SCHPO
ID BGS1_SCHPO Reviewed; 1729 AA.
AC Q10287;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=1,3-beta-glucan synthase component bgs1;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase;
GN Name=bgs1; Synonyms=cps1, drc1; ORFNames=SPBC19G7.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=9401022; DOI=10.1128/jb.179.24.7653-7662.1997;
RA Ishiguro J., Saitou A., Duran A., Ribas J.C.;
RT "cps1+, a Schizosaccharomyces pombe gene homolog of Saccharomyces
RT cerevisiae FKS genes whose mutation confers hypersensitivity to cyclosporin
RT A and papulacandin B.";
RL J. Bacteriol. 179:7653-7662(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=10545452; DOI=10.1093/genetics/153.3.1193;
RA Liu J., Wang H., McCollum D., Balasubramanian M.K.;
RT "Drc1p/Cps1p, a 1,3-beta-glucan synthase subunit, is essential for division
RT septum assembly in Schizosaccharomyces pombe.";
RL Genetics 153:1193-1203(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10503548; DOI=10.1007/s004380051071;
RA Le Goff X., Woollard A., Simanis V.;
RT "Analysis of the cps1 gene provides evidence for a septation checkpoint in
RT Schizosaccharomyces pombe.";
RL Mol. Gen. Genet. 262:163-172(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11054821;
RX DOI=10.1002/1097-0061(200011)16:15<1405::aid-yea625>3.0.co;2-h;
RA Xiang Z., Moore K., Wood V., Rajandream M.A., Barrell B.G., Skelton J.,
RA Churcher C.M., Lyne M.H., Devlin K., Gwilliam R., Rutherford K.M.,
RA Aves S.J.;
RT "Analysis of 114 kb of DNA sequence from fission yeast chromosome 2
RT immediately centromere-distal to his5.";
RL Yeast 16:1405-1411(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-784 AND SER-788, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Required for the assembly of the division septum and
CC maintenance of cell polarity. {ECO:0000269|PubMed:10545452}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
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DR EMBL; D78352; BAA11369.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA17059.1; -; Genomic_DNA.
DR PIR; T43403; T43403.
DR RefSeq; NP_595971.1; NM_001021879.2.
DR AlphaFoldDB; Q10287; -.
DR BioGRID; 277260; 47.
DR STRING; 4896.SPBC19G7.05c.1; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR iPTMnet; Q10287; -.
DR MaxQB; Q10287; -.
DR PaxDb; Q10287; -.
DR PRIDE; Q10287; -.
DR EnsemblFungi; SPBC19G7.05c.1; SPBC19G7.05c.1:pep; SPBC19G7.05c.
DR GeneID; 2540737; -.
DR KEGG; spo:SPBC19G7.05c; -.
DR PomBase; SPBC19G7.05c; bgs1.
DR VEuPathDB; FungiDB:SPBC19G7.05c; -.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000844_0_1_1; -.
DR InParanoid; Q10287; -.
DR OMA; LWFWITV; -.
DR PhylomeDB; Q10287; -.
DR PRO; PR:Q10287; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IC:PomBase.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:1902716; C:cell cortex of growing cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0032154; C:cleavage furrow; IDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0035840; C:old growing cell tip; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IMP:PomBase.
DR GO; GO:0046527; F:glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0000747; P:conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; TAS:PomBase.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:PomBase.
DR GO; GO:0051278; P:fungal-type cell wall polysaccharide biosynthetic process; IMP:PomBase.
DR GO; GO:0031671; P:primary cell septum biogenesis; IGI:PomBase.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Glycosyltransferase; Membrane; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1729
FT /note="1,3-beta-glucan synthase component bgs1"
FT /id="PRO_0000121721"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1180..1200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1237..1257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1337..1357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1440..1460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1484..1504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1515..1535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1550..1572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1678..1698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1729 AA; 199670 MW; B3CABD2960201AC1 CRC64;
MDQYWREQEG RGLFEDDANS YVSDDDTMSS LTRMIYDKNS SRDALHSDYD SSSFNVDSSS
VAYPAWNQAG EEAPVTMEGV QEILLDLTNK LGFQKDNMRN IFDYVMVLLD SRASRMSPSS
ALLTIHADVI GGEHANFSKW YFASHFNDGH AIGFHDMSSP IVETMTLKEA EQAWRDQMAA
FSPHRMMVQV CLYFLCWGEA NNVRFVPECL CFIFECAYDY YISSEAKDVD AALPKEFYLD
SVITPIYRFI HAQLFEILDG KYVRRERDHS QIIGYDDINQ LFWSYKGLQE IMCADKTPLL
DLPPFMRYRH LSDVEWKSCF YKSYYEYRSW FHNVTNFSRI WVMHISAYWY YSAYNSPNLY
TKNYHIRLNN KPPASCRWTA CGLAGAIASF ITLAAVVFEY IHVPRRYHSA RRLWPSMLLL
ISTLLLNIAP VVFIFASSTK EQHYASRLVV GIVHFFFSLV CVVYYSITPL RNLVGFTTKR
SGKNLANRFF TANFTPTSKT GAFVSWCLWI TVLVAKFLES YFFLTLNLAD SIRFLGAMRP
YDCRDYILGA GLCKAQPKIL LSLLYLTDLS LFFLDTYLWY ILISTIYSLA YAFCLGISVW
TPWRELFYRV PRRIYTKLLY TDDMEIVFKP KVLISQVWNA IIISMYREHL ISRTQIQELL
YHQVPSEKAG YHTLRAPNFF YSQQVKHYKQ DLFPANSEAA RRISFFAQSL AESIPKTSSI
DAMPTFTVLV PHYSEKILLS LREIIREEDQ LSRVTLLEYL KQLYPVEWRN FVDDTKLLAD
ENDSVIGSID NEKNGVNKAY DLPFYCVGFK SATPEYTLRT RIWASLRTQT LYRTINGFSN
YSRAIKLLYR TETPELVEWT NGDPVRLDEE LDLMANRKFR FCVSMQRYAK FTKEEAENAE
FLLRAYPDLQ IAYMDEDPQS RHNDERHLYS VLIDGHCPIM ENGKRRPKYR IRLSGNPILG
DGKSDNQNMS IPYIRGEYVQ MIDANQDNYL EECLKIRSIL AEFEQLTPPL HSPYSVNAKA
ADNHPVAILG AREYIFSENT GMLGDVAAGK EQTFGTLFAR ILSLIGGKLH YGHPDFINVL
FMITRGGVSK AQKGLHVNED IYAGMIALQR GGRIKHCDYY QCGKGRDLGF GSILNFTTKI
GTGMAEQMLS REYFNLGTQL PFDRFLSFFY AHAGFHVNNM VIMFSLQLLM LVIINLGAMY
TVVPVCRYRQ FDSLTASLYP EGCYQLKPVL EWLKRCILSI FIVFGIAFVP LAVCELGERG
AIRMVIRLAK QIFSLSPIFE IFTCQIYAQS LIANLTFGGA RYIGTSRGFA TVRVPFSLLY
SRFSGPSLYF GSRLMYMLLF GSITAWLPHY IYFWITLTAL CISPFLYNPH QFAWTDFFVD
YREFMRWLFR ENSRNQANSW IGNCQLCRTR VTGYKRKIYG KKADKIAMDS PRARITTMFY
GEILGPLGTL FFTCIPFLFI NSQPGNDDET QSTNAFIRLI IMSVAPLVLS AIIAFFFFCL
GIMLRPILGD RSKTYGVYLA GVAHFLFVCV DVVVFEVLGY LEGWSFSKTL LGFVAIISIH
RFAHKFFIIC FLSREFRHDG ANLAWWSGRW NGQGFGYMVL TQPWREFVCK TTELNMFAGD
FLLSHLLLFL QAPVILIPYI DKLHSIILFW LVPSRQIRPP IYTIRQNKLR RQIVLRYATL
YFSLFIAFFV LLILPFVFGK SAAGTSMDKF NLIQPATKIV YSSTKNSSV
