ID   BCSB_XANAC              Reviewed;         788 AA.
AC   P58933;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Cyclic di-GMP-binding protein;
DE   AltName: Full=Cellulose synthase regulatory subunit;
DE   Flags: Precursor;
GN   Name=bcsB; OrderedLocusNames=XAC3517;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: Binds the cellulose synthase activator, bis-(3'-5') cyclic
CC       diguanylic acid (c-di-GMP). {ECO:0000250}.
CC   -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC   -!- SUBUNIT: Tightly associated with the cellulose synthase catalytic
CC       subunit. {ECO:0000250}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM38360.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008923; AAM38360.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011052329.1; NC_003919.1.
DR   AlphaFoldDB; P58933; -.
DR   SMR; P58933; -.
DR   STRING; 190486.XAC3517; -.
DR   EnsemblBacteria; AAM38360; AAM38360; XAC3517.
DR   GeneID; 66912554; -.
DR   KEGG; xac:XAC3517; -.
DR   eggNOG; COG1215; Bacteria.
DR   HOGENOM; CLU_003556_1_1_6; -.
DR   OMA; FQYMNPM; -.
DR   UniPathway; UPA00694; -.
DR   Proteomes; UP000000576; 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: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   3: Inferred from homology;
KW   c-di-GMP; Cell inner membrane; Cell membrane; Cellulose biosynthesis;
KW   Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..788
FT                   /note="Cyclic di-GMP-binding protein"
FT                   /id="PRO_0000000272"
FT   TOPO_DOM        35..752
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        753..773
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        774..788
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   788 AA;  85170 MW;  08D7ADF415D02BBC CRC64;
     MRGVSVCFTR TQLMRMFPAV LSCALTLLAG LAQAQQPMPA TPSAQAGSQM QAATPSQVPV
     AFAAAPLPGG STRAATLREL GIDYEITLRG VQGSAGVPFS VRSDEIVTAA TLNLKYSYSP
     SLLPDLSHLK VTINGVTVAT LPTDKANAGK LLSADLPIDP RLVTDYNQLN LQLIGHYTRD
     CEDPDHSSLW ANVDAATSLS LTTTPLALAN NLALLPVPFF DMRDTRRLEL PFYFPQRPDT
     ATLQAAGTVA SWFGSLAGYR GAVFPASTEA LPASGNAVVF ATPGTLPAQF ATADSGVADI
     RGPTVAVLAN PNDRNGKLLL VLGRNSEDLQ RAATALALRA PLTGAVARIG DISAPAPRRP
     YDAPSWVSSE RPVRFGDLVT QPSQLNVAGY HPDLIRIGLQ LPPDLFVWKR DGIPVALNYR
     YTLPEQDNKS ALNVSINESF LTTLPLTGRP FAQSTPMRWW NSLGTRGSMP VHQDLTLPVG
     AFSANSQLRF HFFFDRPQGE ACKNTFPDVS GAIDADSTID LSGFHHYMAM PNLAAFANAG
     YPFTRLADLS ESTIVLPDNP GDQDLSNVLT LLGHFGASTG YPALHAQIIG AGAVQQHAGR
     DLLLLGSAES QPLFKQWRAH LPIGQDGQAT RFALTDWLFE RLPRFLSFDA RRTDLPTTAE
     IALQPQPDDV LLMGFESPLK SGRSVVAFQT EDPANMSRLF DAWFDPTLLK DFQGSVVLLQ
     QNNVTSLVGN QTYYVGHLPL PTWLRWYFSH HPVWLAFTVV LLALLLALAA RVLLRRRTAE
     RLNDGGGA