ID   BCSE_SALT1              Reviewed;         523 AA.
AC   A0A0F6B8A2;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Cyclic di-GMP binding protein BcsE {ECO:0000303|PubMed:24942809};
DE   AltName: Full=Cellulose biosynthesis protein BcsE;
GN   Name=bcsE; OrderedLocusNames=STM14_4362;
OS   Salmonella typhimurium (strain 14028s / SGSC 2262).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=588858;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14028s / SGSC 2262;
RX   PubMed=19897643; DOI=10.1128/jb.01233-09;
RA   Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT   "Short-term signatures of evolutionary change in the Salmonella enterica
RT   serovar typhimurium 14028 genome.";
RL   J. Bacteriol. 192:560-567(2010).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=14028 / UMR1;
RX   PubMed=24942809; DOI=10.1111/mmi.12672;
RA   Fang X., Ahmad I., Blanka A., Schottkowski M., Cimdins A., Galperin M.Y.,
RA   Roemling U., Gomelsky M.;
RT   "GIL, a new c-di-GMP-binding protein domain involved in regulation of
RT   cellulose synthesis in enterobacteria.";
RL   Mol. Microbiol. 93:439-452(2014).
CC   -!- FUNCTION: Binds bis-(3'-5') cyclic diguanylic acid (c-di-GMP) (By
CC       similarity). Required for maximal cellulose synthesis, does not act as
CC       a protease on BcsA (PubMed:24942809). {ECO:0000250|UniProtKB:P37657,
CC       ECO:0000269|PubMed:24942809}.
CC   -!- DISRUPTION PHENOTYPE: Produces much less cellulose, and the timing
CC       cellulose synthesis and structure of the fibers may be altered.
CC       Deletion can be complemented by the protein from S.typhimurium LT2 or
CC       E.coli, however the 'D-415' mutation in the E.coli protein does not
CC       complement (PubMed:24942809). {ECO:0000269|PubMed:24942809}.
CC   -!- SIMILARITY: Belongs to the BcsE family. {ECO:0000305}.
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DR   EMBL; CP001363; ACY90750.1; -; Genomic_DNA.
DR   RefSeq; WP_001205771.1; NZ_CP043402.1.
DR   AlphaFoldDB; A0A0F6B8A2; -.
DR   SMR; A0A0F6B8A2; -.
DR   EnsemblBacteria; ACY90750; ACY90750; STM14_4362.
DR   KEGG; seo:STM14_4362; -.
DR   PATRIC; fig|588858.6.peg.3982; -.
DR   HOGENOM; CLU_039389_2_0_6; -.
DR   OMA; GCGANMV; -.
DR   BioCyc; SENT588858:STM14_RS19165-MON; -.
DR   Proteomes; UP000002695; Chromosome.
DR   GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR017745; BcsE.
DR   Pfam; PF10995; CBP_GIL; 1.
DR   TIGRFAMs; TIGR03369; cellulose_bcsE; 1.
PE   3: Inferred from homology;
KW   Cellulose biosynthesis; Nucleotide-binding.
FT   CHAIN           1..523
FT                   /note="Cyclic di-GMP binding protein BcsE"
FT                   /id="PRO_0000441759"
SQ   SEQUENCE   523 AA;  59307 MW;  626FAD1EACE33420 CRC64;
     MRDTVDPVFS LGISSLWDEL RHMPTGGVWW VNADRQQDAI SLVNQTIASQ TENANVAVIG
     MEGDPGKVIK LDESHGPEKI RLFTMPDSEK GLYSLPHDLL CSVNPTHYFF ILICANNTWR
     NITSESLHKW LEKMNKWTRF HHCSLLVINP CNNSDKQSSL LMGEYRSLFG LASLRFQGDQ
     HLFDIAFWCN EKGVSARQQL LLCQQDERWT LSHQEETAIQ PRSDEKRILS HVAVLEGAPP
     LSEHWTLFDN NEALFNDART AQAATIIFSL TQNNQIEPLA RRIHTLRRQR GSALKIVVRE
     NIASLRATDE RLLLGCGANM IIPWNAPLSR CLTLIESVQG QQFSRYVPED ITTLLSMTQP
     LKLRGFQPWD TFCDAIHTMM SNTLLPADGK GVLVALRPVP GIRVEQALTL CRPNRTGDIM
     TIGGNRLVLF LSFCRVNDLD TALNHIFPLP TGDIFSNRMV WFEDKQISAE LVQMRLLSPE
     LWGTPLPLAK RADPVINAEH DGRIWRRIPE PLRLLDDTAE RAS