ID   BCSB1_KOMXY             Reviewed;         802 AA.
AC   P37716;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Cyclic di-GMP-binding protein;
DE   AltName: Full=CDGBP;
DE   AltName: Full=Cellulose synthase regulatory subunit;
DE            Short=Cellulose synthase protein B;
DE   Flags: Precursor;
GN   Name=bcsB;
OS   Komagataeibacter xylinus (Gluconacetobacter xylinus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Komagataeibacter.
OX   NCBI_TaxID=28448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1306-3;
RX   PubMed=2146681; DOI=10.1073/pnas.87.20.8130;
RA   Wong H.C., Fear A.L., Calhoon R.D., Eichinger G.H., Mayer R., Amikam D.,
RA   Benziman M., Gelfand D.H., Meade J.H., Emerick A.W., Bruner R.,
RA   Ben-Bassat A., Tal R.;
RT   "Genetic organization of the cellulose synthase operon in Acetobacter
RT   xylinum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:8130-8134(1990).
RN   [2]
RP   CHARACTERIZATION, AND PROTEIN SEQUENCE OF 25-42 AND 196-205.
RC   STRAIN=1306-3;
RX   PubMed=1647035; DOI=10.1073/pnas.88.12.5472;
RA   Mayer R., Ross P., Weinhouse H., Amikam D., Volman G., Ohana P.,
RA   Calhoon R.D., Wong H.C., Emerick A.W., Benziman M.;
RT   "Polypeptide composition of bacterial cyclic diguanylic acid-dependent
RT   cellulose synthase and the occurrence of immunologically crossreacting
RT   proteins in higher plants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:5472-5476(1991).
CC   -!- FUNCTION: Binds the cellulose synthase activator, bis-(3'-5') cyclic
CC       diguanylic acid (c-di-GMP).
CC   -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC   -!- SUBUNIT: Tightly associated with the cellulose synthase catalytic
CC       subunit.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AcsB/BcsB family. {ECO:0000305}.
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DR   EMBL; M37202; AAA21885.1; -; Genomic_DNA.
DR   PIR; B43735; B43735.
DR   AlphaFoldDB; P37716; -.
DR   SMR; P37716; -.
DR   STRING; 1220579.GCA_001571345_00313; -.
DR   UniPathway; UPA00694; -.
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:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR   InterPro; IPR003920; Cell_synth_B.
DR   InterPro; IPR018513; Cell_synthase_bac.
DR   PANTHER; PTHR39083; PTHR39083; 1.
DR   Pfam; PF03170; BcsB; 1.
DR   PRINTS; PR01440; CELLSNTHASEB.
PE   1: Evidence at protein level;
KW   c-di-GMP; Cell inner membrane; Cell membrane; Cellulose biosynthesis;
KW   Direct protein sequencing; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..802
FT                   /note="Cyclic di-GMP-binding protein"
FT                   /id="PRO_0000000265"
FT   TOPO_DOM        19..764
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        765..785
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        786..802
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          23..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        197
FT                   /note="C -> G (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        198
FT                   /note="T -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   802 AA;  85382 MW;  79C9320A731B78F8 CRC64;
     MKMVSLIALL VFATGAQAAP VASKAPAPQP AGSDLPPLPA AASQAATPAA ASADQPATTA
     PAADAASASA ADAVVDNAEN AIAASDVATV HTYSLKELGA QSALKMQGAA TLQGLQFGIP
     ADQLVTSARL IVSGAMSPSL QPDTSAVTIT LNEQFIGTLR PDPTHPTFGP LSFDINPIFF
     ITGNRLNFSF ASSSKGCTDP SNGLLWASVS EHSELQITTI PLPPRRQLSR LPQPFFDKNV
     KQKIVIPFVL AQTFDPEVLK ATGILASWFG QQTDFRGVTF PVFSTIPQTG NAVVVGVADE
     LPSALGRQAV NGPTLMEVAN PSDPNGTVLL VTGRDRDEVI TASKGIGFGS SALPTANRMD
     VAPIDVGARV AYDAPSFIPT NRPVRLGELV PDSALQAQGY APGALSVPFR VSPDLYTWRD
     RPYKLNVRFR APPGPIVDVS RSSLNVGIND TYLEAYPLRE PDSTLDQILR RVGLGRGDDS
     VQKHTMPIPP YRVFGQNQLL FYFEMAAMAE PGCKPGPSTF HMSVDPDSTI DLSNSYHITR
     MPNLAFMASA GYPFTTYADL SRSAVVLPDH PNGMVVSAYL DLMGFMGATT WYPVSGVDVV
     SSDHVNDVAD RNLIVLSTLA NSGDVSQLLS KSSYQISDGR LHMGLRSTLS GVWNLFQDPM
     SGISNTAPTD VESTLTGGVA AMIEAESPLA SGRTVLALLS GDGQGLNNLV QILAQRKNQA
     KIQGDLVLAH GDDLTSYRSS PLYTVGTVPL WLEPDWYMHN HPSRVIVVGL LGCILIVAVM
     VRALAKHALR RRRELQEERQ RT