ID   CBPA_CLOCL              Reviewed;        1848 AA.
AC   P38058;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Cellulose-binding protein A;
DE   Flags: Precursor;
GN   Name=cbpA;
OS   Clostridium cellulovorans.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1493;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1565642; DOI=10.1073/pnas.89.8.3483;
RA   Shoseyov O., Takagi M., Goldstein M.A., Doi R.H.;
RT   "Primary sequence analysis of Clostridium cellulovorans cellulose binding
RT   protein A.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:3483-3487(1992).
CC   -!- FUNCTION: Binds to cellulose fibers and coordinates cellulase enzymes.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Remains at the cell surface.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: Glycosylated. {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; M73817; AAA23218.1; -; Genomic_DNA.
DR   PIR; A44140; A44140.
DR   AlphaFoldDB; P38058; -.
DR   SMR; P38058; -.
DR   CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 4.
DR   Gene3D; 2.60.40.710; -; 1.
DR   InterPro; IPR005102; Carbo-bd_X2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR001956; CBM3.
DR   InterPro; IPR036966; CBM3_sf.
DR   InterPro; IPR002102; Cohesin_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF03442; CBM_X2; 4.
DR   Pfam; PF00963; Cohesin; 9.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF49384; SSF49384; 10.
DR   SUPFAM; SSF81296; SSF81296; 4.
DR   PROSITE; PS51172; CBM3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Cellulose degradation; Glycoprotein; Polysaccharide degradation; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..1848
FT                   /note="Cellulose-binding protein A"
FT                   /id="PRO_0000020846"
FT   DOMAIN          29..190
FT                   /note="CBM3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   DOMAIN          291..428
FT                   /note="Cohesin 1"
FT   DOMAIN          435..570
FT                   /note="Cohesin 2"
FT   DOMAIN          668..801
FT                   /note="Cohesin 3"
FT   DOMAIN          810..943
FT                   /note="Cohesin 4"
FT   DOMAIN          952..1085
FT                   /note="Cohesin 5"
FT   DOMAIN          1094..1227
FT                   /note="Cohesin 6"
FT   DOMAIN          1236..1369
FT                   /note="Cohesin 7"
FT   DOMAIN          1377..1511
FT                   /note="Cohesin 8"
FT   DOMAIN          1709..1847
FT                   /note="Cohesin 9"
SQ   SEQUENCE   1848 AA;  189152 MW;  85FA6CE6F771AF1A CRC64;
     MQKKKSLNLL LALMMVFALV LPSIPALAAT SSMSVEFYNS NKSAQTNSIT PIIKITNTSD
     SDLNLNDVKV RYYYTSDGTQ GQTFWCDHAG ALLGNSYVDN TSKVTANFVK ETASPTSTYD
     TYVEFGFASG RATLKKGQFI TIQGRITKSD WSNYTQTNDY SFDASSSTPV VNPKVTGYIG
     GAKVLGTAPG PDVPSSIINP TSATFDKNVT KQADVKTTMT LNGNTFKTIT DANGTALNAS
     TDYSVSGNDV TISKAYLAKQ SVGTTTLNFN FSAGNPQKLV ITVVDTPVEA VTATIGKVQV
     NAGETVAVPV NLTKVPAAGL ATIELPLTFD SASLEVVSIT AGDIVLNPSV NFSSTVSGST
     IKLLFLDDTL GSQLITKDGV FATITFKAKA ITGTTAKVTS VKLAGTPVVG DAQLQEKPCA
     VNPGTVTINP IDNRMQISVG TATVKAGEIA AVPVTLTSVP STGIATAEAQ VSFDATLLEV
     ASVTAGDIVL NPTVNFSYTV NGNVIKLLFL DDTLGSQLIS KDGVFVTINF KAKAVTSTVT
     TPVTVSGTPV FADGTLAEVQ SKTAAGSVTI NIGDPILEPT ISPVTATFDK KAPADVATTM
     TLNGYTFNGI TGLTTSDYSI SGNVVKISQA YLAKQPVGDL TLTFNFSNGN KTATAKLVVS
     IKDAPKTVTA TVGTATVNAG ETVAVPVTLS NVSGISTAEL QLSFDATLLE VVSITAGDIV
     LNPSVNFSSV VNGSTIKLLF LDDTLGSQLI SKDGVFATIN FKAKSVTSTV TTPVKVSGTP
     VFADGTLAEL SYETVAGSVT INAIGPVKTV TATVGTATVK SGETVAVPVT LSNVPGIATA
     ELQLSFDATL LEVASITVGD IVLNPSVNFS SVVNGSTIKL LFLDDTLGSQ LISKDGVLAT
     INFKAKTVTS TVTTPVAVSG TPVFADGTLA ELQSKTVAGS VTIEPSQPVK TVTATVGTAT
     VKSGETVAVP VTLSNVPGIA TAELQVGFDA TLLEVASITV GDIVLNPSVN FSSVVNGSTI
     KLLFLDDTLG SQLISKDGVL ATINFKAKTV TSKVTTPVAV SGTPVFADGT LAELNMKTVA
     GSVTIEPSQP VKTVTATVGT ATVKSGETVA VPVTLSNVPG IATAELQVGF DATLLEVASI
     TVGDIVLNPS VNFSSVVNGS TIKLLFLDDT LGSQLISKDG VLATINFKAK TVTSKVTTPV
     AVSGTPVFAD GTLAELKYET VAGSVTIEPS QPVKTVTATV GTATGKVGET VAVPVTLSNV
     PGIATAEVQV GFDATLLEVA SITAGDIVLN PSVNFSSVVN GSTIKILFLD DTLGSQLISK
     DGVFATINFK IKAVPSTGTT PVAISGTPVF ADGTLAEVQY KTVAGSVTIA AADIKAVKAT
     VGTATGKAGD TVAVPVTLSN VSGIATVELQ LSFDATLLEV ASITAGDIVL NPSVNFSSVV
     NGSTIKILFL DDTLGSQLIS KDGVFATVNF KVKSTATNSA VTPVTVSGTP VFADGTLAEL
     KSESAAGRLT ILPTVIIVDS TVAPTAVTFD KANQADAAIT MTLNGNTFSA IKNGTATLVK
     GTDYTVSENV VTISKAYLAK QTGTVTLEFV FDKGNSAKVV VAVKEIQIVN STITPVVATF
     EKTAAKQADV VVTMSLNGNT FSAIKNGTTT LVKGTDYTIS GSTVTISKAY LATLADGSAT
     LEFVFNQGAS AKLRLTIVPA VVDPVVTDFA VKIDKVSAAA GSTVKVPVSL INVSKVGNVC
     VAEYKISFDS SVLTYVGTTA GTSIKNPAVN FSSQLNGNTI TLLFFDNTIG NELITADGQF
     ATIEFKVNAA ATSGTTAEVK VATISSFADA SLTEITKVAT VNGSVKVS