ID   CIPB_ACETH              Reviewed;         772 AA.
AC   Q01866;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Cellulosomal-scaffolding protein B;
DE   AltName: Full=Cellulose-integrating protein B;
DE   AltName: Full=Cellulosomal glycoprotein S1/SL;
DE   Flags: Fragment;
GN   Name=cipB;
OS   Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium
OS   thermocellum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=1515;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YS;
RX   PubMed=1490597; DOI=10.1016/0378-1097(92)90022-g;
RA   Poole D.M., Morag E., Lamed R., Bayer E.A., Hazlewood G.P., Gilbert H.J.;
RT   "Identification of the cellulose-binding domain of the cellulosome subunit
RT   S1 from Clostridium thermocellum YS.";
RL   FEMS Microbiol. Lett. 78:181-186(1992).
CC   -!- FUNCTION: Acts as a scaffolding protein in the cellulosome. It promotes
CC       binding of cellulose to the catalytic domains of the cellulolytic
CC       enzymes probably through the binding of the nine repeated domains with
CC       dockerin domains present in catalytic subunits of the cellulosome.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Remains at cell surface.
CC   -!- DOMAIN: The cohesin domains bind to the dockerin domain born by the
CC       catalytic components of the cellulosome.
CC   -!- PTM: O-glycosylated on most but not all Thr residues of the linker
CC       units. {ECO:0000250}.
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DR   EMBL; X68233; CAA48312.1; -; Genomic_DNA.
DR   PDB; 2B59; X-ray; 2.11 A; B=-.
DR   PDBsum; 2B59; -.
DR   AlphaFoldDB; Q01866; -.
DR   SMR; Q01866; -.
DR   CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR   EvolutionaryTrace; Q01866; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; 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; 2.60.40.710; -; 1.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
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; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF00963; Cohesin; 3.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF49384; SSF49384; 4.
DR   SUPFAM; SSF49464; SSF49464; 1.
DR   SUPFAM; SSF63446; SSF63446; 1.
DR   PROSITE; PS51172; CBM3; 1.
DR   PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Cellulose degradation; Glycoprotein; Polysaccharide degradation; Repeat;
KW   Secreted.
FT   CHAIN           <1..772
FT                   /note="Cellulosomal-scaffolding protein B"
FT                   /id="PRO_0000089767"
FT   DOMAIN          <1..80
FT                   /note="Cohesin 1"
FT   DOMAIN          94..240
FT                   /note="Cohesin 2"
FT   DOMAIN          277..435
FT                   /note="CBM3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   DOMAIN          462..607
FT                   /note="Cohesin 3"
FT   DOMAIN          704..771
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT   REGION          81..93
FT                   /note="Linker (Pro/Thr-rich)"
FT   REGION          235..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..272
FT                   /note="Linker (Pro/Thr-rich)"
FT   REGION          438..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..461
FT                   /note="Linker (Pro/Thr-rich)"
FT   COMPBIAS        236..277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..461
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   772 AA;  82492 MW;  BBF06DE5E094FE10 CRC64;
     DPSKSFDSAI YPDRKMIVFL FAEDSGRGTY AITQDGVFAT IVATVKSAAA APITLLEVGA
     FRDNDLVEIS TTFVAGGVNL GSSVPTTQPN VPSDGVVVEI GKVTGSVGTT VEIPVYFRGV
     PSKGIANCDF VFRYDPNVLE IIGIDPRSII VDPNPTKSFD TAIYADRKII VFLFCGRQRN
     RSVSITKDGV FAKIRATVKS SAPAYITFDE VGGFADNDLV EQKVSFIDGG VNVGNATPTK
     GATPTNTATP TKSATATPPG HSVPTNTPTN TPANTPVSGN LKVEFYNSNP SDTTNSINPQ
     FKVTNTGSSA IDLSKLTLRY YYTVDGQKDQ TFWCDHAAII GSNGSYNGIT SNVKGTFVKM
     SSSTNNADTY LEISFTGGTL EPGAHVQIQG RFAKNDWSNY TQSNDYSFKS RSQFVEWDQV
     TAYLNGVLVW GKEPGGSVVP STQPVTTPPA TTKPPATTIP PSDDPNAIKI KVDTVNAKPG
     DTVNIPVRFS GIPSKGIANC DFVYSYDPNV LEIIEIKPGE LIVDPNPDKS FDTAVYPDRK
     MIVFLFAEDS GTGAYAITED GVFATIVAKV KEGAPEGFSA IEISEFGAFA DNDLVEVETD
     LINGGVLVTN KPVIEGYKVS GYILPDFSFD ATVAPLVKAG FKVEIVGTEL YAVTDANGYF
     EITGVPANAS GYTLKISRAT YLDRVIANVV VTGDTSVSTS QAPIMMWVGD IVKDNSINLL
     DVAEVIRCFN ATKGSANYVE ELDINRNGAI NMQDIMIVHK HFGATSSDYD AQ