EPSI_BACSU
ID EPSI_BACSU Reviewed; 358 AA.
AC P71058; O08177; Q795I7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Putative pyruvyl transferase EpsI;
DE EC=2.-.-.-;
GN Name=epsI; Synonyms=yveS; OrderedLocusNames=BSU34290;
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 -!- INDUCTION: Repressed by SinR. {ECO:0000269|PubMed:15661000}.
CC -!- SIMILARITY: Belongs to the polysaccharide pyruvyl transferase family.
CC {ECO:0000305}.
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DR EMBL; Z71928; CAA96476.1; -; Genomic_DNA.
DR EMBL; Z94043; CAB08031.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15434.1; -; Genomic_DNA.
DR PIR; H70036; H70036.
DR RefSeq; NP_391309.1; NC_000964.3.
DR RefSeq; WP_003228262.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P71058; -.
DR SMR; P71058; -.
DR STRING; 224308.BSU34290; -.
DR PaxDb; P71058; -.
DR PRIDE; P71058; -.
DR EnsemblBacteria; CAB15434; CAB15434; BSU_34290.
DR GeneID; 937256; -.
DR KEGG; bsu:BSU34290; -.
DR PATRIC; fig|224308.179.peg.3715; -.
DR eggNOG; COG5039; Bacteria.
DR InParanoid; P71058; -.
DR OMA; HGMIFCA; -.
DR PhylomeDB; P71058; -.
DR BioCyc; BSUB:BSU34290-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR007345; Polysacch_pyruvyl_Trfase.
DR Pfam; PF04230; PS_pyruv_trans; 1.
PE 2: Evidence at transcript level;
KW Exopolysaccharide synthesis; Reference proteome; Transferase.
FT CHAIN 1..358
FT /note="Putative pyruvyl transferase EpsI"
FT /id="PRO_0000360701"
SQ SEQUENCE 358 AA; 41509 MW; E96B1150E9D57C34 CRC64;
MSLQSLKINF AEWLLLKVKY PSQYWLGAAD QPVKAAAHQK KIILTLLPSH DNLGDHAIAY
ASKAFLEQEY PDFDIVEVDM KDIYKSAKSL IRSRHPEDMV FIIGGGNMGD LYRYEEWTRR
FIIKTFHDYR VVQLPATAHF SDTKKGRKEL KRAQKIYNAH PGLLLMARDE TTYQFMKQHF
QEKTILKQPD MVLYLDRSKA PAEREGVYMC LREDQESVLQ EEQRNRVKAA LCEEFGEIKS
FTTTIGRRVS RDTREHELEA LWSKLQSAEA VVTDRLHGMI FCALTGTPCV VIRSFDHKVM
EGYQWLKDIP FMKLIEHPEP ERVTAAVNEL LTKETSRAGF PRDVYFKGLR DKISGEAQ
