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 03-MAY-2023, entry version 116.
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; Bacillota; 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 CDD; cd14253; Dockerin; 1.
DR CDD; cd08548; Type_I_cohesin_like; 3.
DR Gene3D; 2.60.40.4130; -; 1.
DR Gene3D; 2.60.40.680; -; 3.
DR Gene3D; 2.60.40.710; Endoglucanase-like; 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; Carbohydrate-binding domain; 4.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 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
//
