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EPSG_BACSU
ID   EPSG_BACSU              Reviewed;         367 AA.
AC   P71056; O08175; Q795I5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Transmembrane protein EpsG;
GN   Name=epsG; Synonyms=yveQ; OrderedLocusNames=BSU34310;
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].
RC   STRAIN=168;
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Repressed by SinR. {ECO:0000269|PubMed:15661000}.
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DR   EMBL; Z71928; CAA96474.1; -; Genomic_DNA.
DR   EMBL; Z94043; CAB08029.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15436.1; -; Genomic_DNA.
DR   PIR; F70036; F70036.
DR   RefSeq; NP_391311.1; NC_000964.3.
DR   RefSeq; WP_003228259.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; P71056; -.
DR   STRING; 224308.BSU34310; -.
DR   TCDB; 9.B.183.1.9; the wzy glycosyltransferase (epsg) family.
DR   PaxDb; P71056; -.
DR   EnsemblBacteria; CAB15436; CAB15436; BSU_34310.
DR   GeneID; 937071; -.
DR   KEGG; bsu:BSU34310; -.
DR   PATRIC; fig|224308.179.peg.3717; -.
DR   eggNOG; ENOG50330DE; Bacteria.
DR   InParanoid; P71056; -.
DR   OMA; ARFNIYF; -.
DR   BioCyc; BSUB:BSU34310-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Cell membrane; Exopolysaccharide synthesis; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..367
FT                   /note="Transmembrane protein EpsG"
FT                   /id="PRO_0000360700"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   367 AA;  42555 MW;  88D37986AFD9C9C6 CRC64;
     MIVYAVNMGI VFIWSWFAKM CGGRDDSLAT GYRPNKLLIW IPLASLVLVS GLRYRVGTDF
     QTYTLLYELA GDYQNVWQIF GFGTAKTATD PGFTALLWLM NFITEDPQIM YFTVAVVTYS
     FIMKTLADYG RPFELSVFLF LGTFHYYASF NGIRQYMVAA VLFWAIRYII SGNWKRYFLI
     VLVSSLFHSS ALIMIPVYFI VRRKAWSPAI FGLSALFLGM TFLYQKFISV FVVVLENSSY
     SHYEKWLMTN TNGMNVIKIA VLVLPLFLAF CYKERLRSLW PQIDIVVNLC LLGFLFGLLA
     TKDVIFARFN IYFGLYQMIL VPYFVRIFDE KSNALIYIAI VVCYFLYSYL LMPVDSSVLP
     YRTIFSR
 
 
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