CBDP_ACET2
ID CBDP_ACET2 Reviewed; 286 AA.
AC A3DHD2;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Carbohydrate-binding domain-containing protein Cthe_2159 {ECO:0000303|PubMed:25286843, ECO:0000312|EMBL:ABN53361.1};
DE AltName: Full=Polysaccharide lyase-like protein Cthe_2159 {ECO:0000303|PubMed:25286843};
DE Short=PL-like protein Cthe_2159 {ECO:0000303|PubMed:25286843};
DE Flags: Precursor;
GN OrderedLocusNames=Cthe_2159 {ECO:0000312|EMBL:ABN53361.1};
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119 {ECO:0000312|EMBL:ABN53361.1};
RN [1] {ECO:0000312|Proteomes:UP000002145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372 {ECO:0000312|Proteomes:UP000002145};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:4PEU, ECO:0007744|PDB:4PHB}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-286 OF GLY-199/GLY-213 MUTANT
RP IN COMPLEX WITH CALCIUM, FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372 {ECO:0000303|PubMed:25286843};
RX PubMed=25286843; DOI=10.1107/s1399004714015934;
RA Close D.W., D'Angelo S., Bradbury A.R.;
RT "A new family of beta-helix proteins with similarities to the
RT polysaccharide lyases.";
RL Acta Crystallogr. D 70:2583-2592(2014).
CC -!- FUNCTION: Binds cellulosic and pectic substrates. Displays no enzyme
CC activity (in vitro). {ECO:0000269|PubMed:25286843}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25286843}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303,
CC ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000568; ABN53361.1; -; Genomic_DNA.
DR RefSeq; WP_020457724.1; NC_009012.1.
DR PDB; 4PEU; X-ray; 1.80 A; A=2-286.
DR PDB; 4PHB; X-ray; 2.18 A; A=2-286.
DR PDBsum; 4PEU; -.
DR PDBsum; 4PHB; -.
DR AlphaFoldDB; A3DHD2; -.
DR SMR; A3DHD2; -.
DR STRING; 203119.Cthe_2159; -.
DR EnsemblBacteria; ABN53361; ABN53361; Cthe_2159.
DR KEGG; cth:Cthe_2159; -.
DR eggNOG; ENOG502Z8AD; Bacteria.
DR HOGENOM; CLU_962080_0_0_9; -.
DR OMA; NACIYSR; -.
DR OrthoDB; 990734at2; -.
DR Proteomes; UP000002145; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0030248; F:cellulose binding; IDA:UniProtKB.
DR GO; GO:0048028; F:galacturonan binding; IDA:UniProtKB.
DR GO; GO:2001062; F:xylan binding; IDA:UniProtKB.
DR InterPro; IPR025584; Cthe_2159.
DR Pfam; PF14262; Cthe_2159; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Lipoprotein; Membrane; Metal-binding;
KW Palmitate; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..286
FT /note="Carbohydrate-binding domain-containing protein
FT Cthe_2159"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_0000434100"
FT REGION 124..225
FT /note="Polygalacturonic acid-binding"
FT /evidence="ECO:0000269|PubMed:25286843"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25286843,
FT ECO:0007744|PDB:4PEU"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25286843,
FT ECO:0007744|PDB:4PEU"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25286843,
FT ECO:0007744|PDB:4PEU"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25286843,
FT ECO:0007744|PDB:4PEU"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25286843,
FT ECO:0007744|PDB:4PEU"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25286843,
FT ECO:0007744|PDB:4PEU"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25286843,
FT ECO:0007744|PDB:4PEU"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25286843,
FT ECO:0007744|PDB:4PEU"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25286843,
FT ECO:0007744|PDB:4PEU"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 69..79
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 91..102
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 147..167
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 169..181
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 194..203
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 234..243
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 267..276
FT /evidence="ECO:0007829|PDB:4PEU"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:4PEU"
SQ SEQUENCE 286 AA; 30131 MW; AA6BB27D94732B0D CRC64;
MSIKKLILAA SILTTLALTG CGGKGAVQPS GVSTGDVNAK IVFDNDKVNA DNVDGLSVSE
REVKITKPGM YTFSGTWNDG QILVDIGKEF EAVLVLDGVN ITNTKSAPIY IKSAEKVKIE
LADGKDNVLT DAEFYEFEDP QDNKPNACIY SRDDITIKGN GNLTVNANFN NGIGTSNDLK
ITGGNITVKA FNNGLKGNDS VTISGGNIDI TAEADGIKVE NTEEPHKGYV NITGGTIKIR
AKDDAIDSVR SVSINNADVK VSVGGKDVKC EGVLNIAEGC LGKLEE
