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Database: UniProt
Entry: A0A0A2W330_BEABA
LinkDB: A0A0A2W330_BEABA
Original site: A0A0A2W330_BEABA 
ID   A0A0A2W330_BEABA        Unreviewed;      2268 AA.
AC   A0A0A2W330;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Cyclic di-GMP-binding protein {ECO:0000256|ARBA:ARBA00021844};
DE   AltName: Full=Cellulose synthase regulatory subunit {ECO:0000256|ARBA:ARBA00033444};
GN   ORFNames=BBAD15_g1221 {ECO:0000313|EMBL:KGQ13032.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ13032.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ13032.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ13032.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds the cellulose synthase activator, bis-(3'-5') cyclic
CC       diguanylic acid (c-di-GMP). {ECO:0000256|ARBA:ARBA00002057}.
CC   -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005186}.
CC   -!- SUBUNIT: Tightly associated with the cellulose synthase catalytic
CC       subunit. {ECO:0000256|ARBA:ARBA00011437}.
CC   -!- SIMILARITY: Belongs to the AcsB/BcsB family.
CC       {ECO:0000256|ARBA:ARBA00010714}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) family.
CC       {ECO:0000256|ARBA:ARBA00009209}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGQ13032.1}.
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DR   EMBL; ANFO01000064; KGQ13032.1; -; Genomic_DNA.
DR   HOGENOM; CLU_230478_0_0_1; -.
DR   UniPathway; UPA00694; -.
DR   Proteomes; UP000030106; Unassembled WGS sequence.
DR   GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR008410; BCSC_C.
DR   InterPro; IPR003920; Cell_synth_B.
DR   InterPro; IPR018513; Cell_synthase_bac.
DR   InterPro; IPR002037; Glyco_hydro_8.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR39083; CYCLIC DI-GMP-BINDING PROTEIN; 1.
DR   PANTHER; PTHR39083:SF1; CYCLIC DI-GMP-BINDING PROTEIN; 1.
DR   Pfam; PF03170; BcsB; 1.
DR   Pfam; PF05420; BCSC_C; 1.
DR   Pfam; PF01270; Glyco_hydro_8; 1.
DR   Pfam; PF14559; TPR_19; 2.
DR   Pfam; PF13181; TPR_8; 1.
DR   PRINTS; PR01440; CELLSNTHASEB.
DR   SMART; SM00028; TPR; 6.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   SUPFAM; SSF48452; TPR-like; 4.
DR   PROSITE; PS50005; TPR; 1.
PE   3: Inferred from homology;
KW   c-di-GMP {ECO:0000256|ARBA:ARBA00022636};
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..2268
FT                   /note="Cyclic di-GMP-binding protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001996376"
FT   REPEAT          1406..1439
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          1908..2248
FT                   /note="Cellulose synthase operon C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05420"
FT   REGION          2173..2202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2268 AA;  250493 MW;  11D739F205B7DFB3 CRC64;
     MKRKISWFYA AAVGISALPV TVANAADTTP APTVPAVATA NQAVITPAPG AAEALVPATP
     ADNAPTVGQV LPGVQGANAP IVAENVPSRD VKLNFAQIAP PPGSMVLTGV NPNGGVEFGM
     RRDEIVSKAL LNLEYTPSPS LLPVQSQLKV YLNDELMGVL PVTKEQLGKK TFAQVPVDPL
     YITDFNRVRL EFVGHYRDIC ENPASTTLWM DVGRSSSLAL TYQRLPVQND LSHFPVPFFD
     SRDDRPLTLP IVFAASPDIE QQRAAGIVAS WFGSRTAWRG QNFPVLFNQL PTSNGIVFAT
     NDKRPDFLRN HPAVQAPTVE MMSHPDNPYV KLLVVMGRDD KDLVQAAKGI AQGNILFRGS
     SVTVDDVKPL LPREPYDAPN WVRTDRPVTL GEMKTYQEQL QSSGQEPSAI SVTMNLPPDL
     YLLRSNGIDL NLKYRYTAPA MKDSSRMDIS LNNQFLQSFN LTPSEENNKL LLRLPVLQGL
     LDGKTDVSIP ALRLGAANQL RFDFSYMNPM PGGSLENCVT FQPVQNHVVV EDESTIDFSN
     YHHFIAMPDL RTFANAGFPF SRMADLSQTI VVVSKEPDPA QVTALLDALG TIGSQTGFPA
     LSVNLTDDGS TIQGKDADIM IIGSIPPALK DDKRIDLLVD ATQSWVKTPV RQTPLLNSVS
     DPKDRAADTQ TAITSQGAMA AIVGFQSPYN DQRSVLALLA DSPRGYELLN SALNDSGKRA
     AISGSVAVIR ESGVDSLRVG DIYYVGHLPW FERIWYALSN HPVLLAIFAA ISVVLLAWVL
     WRILRILSRR RIDPEDDYVS DQGRVIDPSD ERKITTSEGQ SYGLFFALAA NDRAMFDQLL
     RWTENNLAQG ALKDHLPAWL WGKNDKDEWT VLDSNSASDA DMWIVWSLLE AGRLWHEPAY
     KRLGEQLLKR VAKEEVIKIP GLGFSLLPGR VGFNHSPDWR LNPSYLPPQV LQRMVRYRGP
     WSAMQVANQR LLLETAAKGF SPNWADWHEG KGWQFQTDDA RYGSYDSIRV YMWVGMMADD
     APHKAALLKA FQPMADITIK QGLPPEKVDV QTGNVQGTGP VGFSAAMLPF LQDSEARDVQ
     RQRVKDNFPQ ADAYYSYVLT LFGQGWDQKR FRFNSLGELI PSWGQAALTP QQQLLEQVRM
     GEASKREDIV RQSLSRLELM APDDPDVIAA RMRYLLRQGD NAGAKAQLER LAKLAPGSAE
     YKQSQVTLML TGADGRQQLQ QARLLAASGH TDQAIAAYEK LFDGNPPEGD LAIEYWMLMA
     KRPATTNQAI DKLKALDAAA PGNAELRGNL ARLMFANGRS AEAYQVLEQM AKSSGSREDA
     AALWYSQISN LPTGPQSVAA LQRFLNVFTE GDTVASARDK LAQQQKQLAD PAFLARAKGL
     EDVGGGRGNQ AIPQLKEALS TKQNDSEVVG ALGQAYSQQG KRALAVQQFE KAIQMDPQSD
     NRGKWDSLLK TNRYWLLIEQ GDAQLKANNP DAALQKYQLA QRIDNTDSYA VLGFGDVAVA
     KKDDASAERY YQQALRMDRG NSNAIRGLAN VYRRQSPERA AAYIQSLSAS QRKSIDDIER
     SLAGERLEQQ ATALESQGQW AKAAEIQRRR LQLDPDSVWI TYRLSNDLYA AGKHSEADSL
     MRGLAQRKPG DPEQVFAYGL YLSGNDHDAA ALSHLNTLPK AQWTDNIHEL ADRLQFNEVM
     QTANRLRDSG KEKDAIALLQ QQTPSDRVDL TLSDWAAERG DRATAKSQYQ KVLQRSPGNE
     DALLGLTEVL IAEGDKPQAR GLLAKLQEAP TGDTPSINTQ RRIANAWAAL GDNEKAAQTY
     APILVAAKTQ PPSMESALVM RDAARFQAAS GQPQQALETY KDAMVSSGIT RQRPQDNDTF
     TRLTRNDEKD DWLKRGVRSD AADLYRQQDV NVTLDHEYWG SSGTPGYSDL KAHTTMLQVD
     APLSDGRMWF RTDMVNMDAG SFKDNGAGYN ERWGTCAKHN CFGNRRQSGN GASVAVGWKN
     NTWQTDIGTT PMGFDVVDVV GGVSYSNDLG PIGYTVNAHR RPISSSLLSF GGQRDPNTKT
     VWGGVRATGG GVSLSYDKGE ANGVWSSLSA DTLTGKNVAD NWRVRWMTGY YYKLINENNQ
     RLTVGLTNMV WHYEKDLSDY FLGQGGYYSP QKYVSFAVPV IWRKRTENWS WELGASGSWS
     YSHSNAGQRY PLRNLVPNNT NDYPEDPYAY PDRNDPSSAS SSNGFGYTAR ALVERRISSH
     WSIGAGIDIQ QAKDYTPSHA LIYVRYSMAG WQGDMDMPPQ PLVPYADF
//
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