ID   EPSF_BACSU              Reviewed;         384 AA.
AC   P71055; O08174; Q795I4;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Putative glycosyltransferase EpsF;
DE            EC=2.4.-.-;
GN   Name=epsF; Synonyms=yveP; OrderedLocusNames=BSU34320;
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=168trp;
RX   PubMed=8969506; DOI=10.1099/13500872-142-11-3089;
RA   Fabret C., Quentin Y., Chapal N., Guiseppi A., Haiech J., Denizot F.;
RT   "Integrated mapping and sequencing of a 115 kb DNA fragment from Bacillus
RT   subtilis: sequence analysis of a 21 kb segment containing the sigL locus.";
RL   Microbiology 142:3089-3096(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Denizot F.;
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   PROBABLE FUNCTION.
RX   PubMed=15175311; DOI=10.1128/jb.186.12.3970-3979.2004;
RA   Branda S.S., Gonzalez-Pastor J.E., Dervyn E., Ehrlich S.D., Losick R.,
RA   Kolter R.;
RT   "Genes involved in formation of structured multicellular communities by
RT   Bacillus subtilis.";
RL   J. Bacteriol. 186:3970-3979(2004).
RN   [5]
RP   PROBABLE FUNCTION, INDUCTION, AND NOMENCLATURE.
RX   PubMed=15661000; DOI=10.1111/j.1365-2958.2004.04440.x;
RA   Kearns D.B., Chu F., Branda S.S., Kolter R., Losick R.;
RT   "A master regulator for biofilm formation by Bacillus subtilis.";
RL   Mol. Microbiol. 55:739-749(2005).
CC   -!- FUNCTION: May be involved in the production of the exopolysaccharide
CC       (EPS) component of the extracellular matrix during biofilm formation.
CC       EPS is responsible for the adhesion of chains of cells into bundles.
CC       Required for biofilm maintenance.
CC   -!- INDUCTION: Repressed by SinR. {ECO:0000269|PubMed:15661000}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR   EMBL; Z71928; CAA96473.1; -; Genomic_DNA.
DR   EMBL; Z94043; CAB08028.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15437.1; -; Genomic_DNA.
DR   PIR; E70036; E70036.
DR   RefSeq; NP_391312.1; NC_000964.3.
DR   RefSeq; WP_003228257.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; P71055; -.
DR   SMR; P71055; -.
DR   STRING; 224308.BSU34320; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PaxDb; P71055; -.
DR   DNASU; 938631; -.
DR   EnsemblBacteria; CAB15437; CAB15437; BSU_34320.
DR   GeneID; 938631; -.
DR   KEGG; bsu:BSU34320; -.
DR   PATRIC; fig|224308.179.peg.3718; -.
DR   eggNOG; COG0438; Bacteria.
DR   InParanoid; P71055; -.
DR   OMA; CACGEDA; -.
DR   PhylomeDB; P71055; -.
DR   BioCyc; BSUB:BSU34320-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR028098; Glyco_trans_4-like_N.
DR   Pfam; PF13439; Glyco_transf_4; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   2: Evidence at transcript level;
KW   Exopolysaccharide synthesis; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..384
FT                   /note="Putative glycosyltransferase EpsF"
FT                   /id="PRO_0000360693"
SQ   SEQUENCE   384 AA;  42623 MW;  7FCA7C9136424710 CRC64;
     MNSSQKRVLH VLSGMNRGGA ETMVMNLYRK MDKSKVQFDF LTYRNDPCAY DEEILSLGGR
     LFYVPSIGQS NPLTFVRNVR NAIKENGPFS AVHAHTDFQT GFIALAARLA GVPVRVCHSH
     NTSWKTGFNW KDRLQLLVFR RLILANATAL CACGEDAGRF LFGQSNMERE RVHLLPNGID
     LELFAPNGQA ADEEKAARGI AADRLIIGHV ARFHEVKNHA FLLKLAAHLK ERGIRFQLVL
     AGDGPLCGEI EEEARQQNLL SDVLFLGTEE RIHELMRTFD VFVMPSLYEG LPVVLVEAQA
     SGLPCIISDS ITEKVDAGLG LVTRLSLSEP ISVWAETIAR AAAAGRPKRE FIKETLAQLG
     YDAQQNVGAL LNVYNISTEK DHNR