CIPA_ACET2
ID CIPA_ACET2 Reviewed; 1853 AA.
AC Q06851; A3DJZ4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cellulosomal-scaffolding protein A;
DE AltName: Full=Cellulose-integrating protein A;
DE AltName: Full=Cellulosomal glycoprotein S1/SL;
DE AltName: Full=Cohesin;
DE Flags: Precursor;
GN Name=cipA; OrderedLocusNames=Cthe_3077;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 29-40 AND 42-43.
RX PubMed=8316083; DOI=10.1111/j.1365-2958.1993.tb01576.x;
RA Gerngross U.T., Romaniec M.P.M., Kobayashi T., Huskisson N.S., Demain A.L.;
RT "Sequencing of a Clostridium thermocellum gene (cipA) encoding the
RT cellulosomal SL-protein reveals an unusual degree of internal homology.";
RL Mol. Microbiol. 8:325-334(1993).
RN [2]
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;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1820-1853.
RX PubMed=8458832; DOI=10.1128/jb.175.7.1891-1899.1993;
RA Fujino T., Beguin P., Aubert J.-P.;
RT "Organization of a Clostridium thermocellum gene cluster encoding the
RT cellulosomal scaffolding protein CipA and a protein possibly involved in
RT attachment of the cellulosome to the cell surface.";
RL J. Bacteriol. 175:1891-1899(1993).
RN [4]
RP GLYCOSYLATION.
RC STRAIN=YS;
RX PubMed=8262930; DOI=10.1016/s0021-9258(19)74203-3;
RA Gerwig G.J., Kamerling J.P., Vliegenthart J.F.G., Morag E., Lamed R.,
RA Bayer E.A.;
RT "The nature of the carbohydrate-peptide linkage region in glycoproteins
RT from the cellulosomes of Clostridium thermocellum and Bacteroides
RT cellulosolvens.";
RL J. Biol. Chem. 268:26956-26960(1993).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 184-321.
RX PubMed=9083107; DOI=10.1016/s0969-2126(97)00195-0;
RA Shimon L.J.W., Bayer E.A., Morag E., Lamed R., Yaron S., Shoham Y.,
RA Frolow F.;
RT "A cohesin domain from Clostridium thermocellum: the crystal structure
RT provides new insights into cellulosome assembly.";
RL Structure 5:381-390(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 368-522.
RX PubMed=8918451; DOI=10.1002/j.1460-2075.1996.tb00960.x;
RA Tormo J., Lamed R., Chirino A.J., Morag E., Bayer E.A., Shoham Y.,
RA Steitz T.A.;
RT "Crystal structure of a bacterial family-III cellulose-binding domain: a
RT general mechanism for attachment to cellulose.";
RL EMBO J. 15:5739-5751(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1213-1361.
RX PubMed=9402065; DOI=10.1006/jmbi.1997.1326;
RA Tavares G.A., Beguin P., Alzari P.M.;
RT "The crystal structure of a type I cohesin domain at 1.7-A resolution.";
RL J. Mol. Biol. 273:701-713(1997).
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.
CC -!- INTERACTION:
CC Q06851; A3DF10: Cthe_1307; NbExp=2; IntAct=EBI-687595, EBI-9021730;
CC Q06851; P51584: xynY; Xeno; NbExp=5; IntAct=EBI-687595, EBI-1037473;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Remains at the 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. The reducing sugar is galactopyranose.
CC {ECO:0000269|PubMed:8262930}.
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; L08665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP000568; ABN54273.1; -; Genomic_DNA.
DR EMBL; X67506; CAA47840.1; -; Genomic_DNA.
DR PIR; S36859; S36859.
DR RefSeq; WP_020458017.1; NC_009012.1.
DR PDB; 1ANU; X-ray; 2.15 A; A=184-321.
DR PDB; 1AOH; X-ray; 1.70 A; A/B=1216-1361.
DR PDB; 1NBC; X-ray; 1.75 A; A/B=368-522.
DR PDB; 1OHZ; X-ray; 2.20 A; A=181-340.
DR PDB; 2B59; X-ray; 2.11 A; B=1691-1853.
DR PDB; 2CCL; X-ray; 2.03 A; A/C=181-328.
DR PDB; 3KCP; X-ray; 1.94 A; A=1542-1853.
DR PDB; 4B9F; X-ray; 1.19 A; A/B=368-519.
DR PDB; 5G5D; X-ray; 3.00 A; B=1691-1853.
DR PDBsum; 1ANU; -.
DR PDBsum; 1AOH; -.
DR PDBsum; 1NBC; -.
DR PDBsum; 1OHZ; -.
DR PDBsum; 2B59; -.
DR PDBsum; 2CCL; -.
DR PDBsum; 3KCP; -.
DR PDBsum; 4B9F; -.
DR PDBsum; 5G5D; -.
DR AlphaFoldDB; Q06851; -.
DR SMR; Q06851; -.
DR DIP; DIP-42322N; -.
DR IntAct; Q06851; 13.
DR MINT; Q06851; -.
DR STRING; 203119.Cthe_3077; -.
DR CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR GlyConnect; 84; 7 O-Linked glycans.
DR EnsemblBacteria; ABN54273; ABN54273; Cthe_3077.
DR KEGG; cth:Cthe_3077; -.
DR eggNOG; COG2911; Bacteria.
DR HOGENOM; CLU_002254_0_0_9; -.
DR OMA; AVYPDRK; -.
DR OrthoDB; 886997at2; -.
DR BioCyc; MetaCyc:MON-16412; -.
DR EvolutionaryTrace; Q06851; -.
DR Proteomes; UP000002145; Chromosome.
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; 9.
DR Pfam; PF00404; Dockerin_1; 1.
DR SMART; SM01067; CBM_3; 1.
DR SUPFAM; SSF49384; SSF49384; 10.
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; Direct protein sequencing; Glycoprotein;
KW Polysaccharide degradation; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:8316083"
FT CHAIN 29..1853
FT /note="Cellulosomal-scaffolding protein A"
FT /id="PRO_0000020932"
FT DOMAIN 29..182
FT /note="Cohesin 1"
FT DOMAIN 183..322
FT /note="Cohesin 2"
FT DOMAIN 365..523
FT /note="CBM3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT DOMAIN 560..704
FT /note="Cohesin 3"
FT DOMAIN 724..866
FT /note="Cohesin 4"
FT DOMAIN 889..1031
FT /note="Cohesin 5"
FT DOMAIN 1054..1196
FT /note="Cohesin 6"
FT DOMAIN 1219..1361
FT /note="Cohesin 7"
FT DOMAIN 1384..1526
FT /note="Cohesin 8"
FT DOMAIN 1548..1690
FT /note="Cohesin 9"
FT DOMAIN 1785..1852
FT /note="Dockerin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT REGION 323..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..363
FT /note="Linker (Pro/Thr-rich)"
FT REGION 523..559
FT /note="Linker (Pro/Thr-rich)"
FT REGION 525..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..555
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1615
FT /note="A -> AA (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:2CCL"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:2CCL"
FT STRAND 213..221
FT /evidence="ECO:0007829|PDB:2CCL"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:2CCL"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:2CCL"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:2CCL"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:2CCL"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:2CCL"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:2CCL"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:2CCL"
FT STRAND 277..286
FT /evidence="ECO:0007829|PDB:2CCL"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1OHZ"
FT STRAND 292..303
FT /evidence="ECO:0007829|PDB:2CCL"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:2CCL"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:2CCL"
FT STRAND 369..376
FT /evidence="ECO:0007829|PDB:4B9F"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:4B9F"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:4B9F"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:4B9F"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:4B9F"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:4B9F"
FT STRAND 418..428
FT /evidence="ECO:0007829|PDB:4B9F"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:4B9F"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:4B9F"
FT STRAND 441..452
FT /evidence="ECO:0007829|PDB:4B9F"
FT STRAND 455..465
FT /evidence="ECO:0007829|PDB:4B9F"
FT STRAND 473..482
FT /evidence="ECO:0007829|PDB:4B9F"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:4B9F"
FT STRAND 508..512
FT /evidence="ECO:0007829|PDB:4B9F"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:4B9F"
FT STRAND 1220..1224
FT /evidence="ECO:0007829|PDB:1AOH"
FT STRAND 1226..1229
FT /evidence="ECO:0007829|PDB:1AOH"
FT STRAND 1234..1243
FT /evidence="ECO:0007829|PDB:1AOH"
FT STRAND 1249..1257
FT /evidence="ECO:0007829|PDB:1AOH"
FT TURN 1260..1262
FT /evidence="ECO:0007829|PDB:1AOH"
FT STRAND 1263..1270
FT /evidence="ECO:0007829|PDB:1AOH"
FT HELIX 1279..1282
FT /evidence="ECO:0007829|PDB:1AOH"
FT STRAND 1283..1288
FT /evidence="ECO:0007829|PDB:1AOH"
FT TURN 1289..1292
FT /evidence="ECO:0007829|PDB:1AOH"
FT STRAND 1293..1299
FT /evidence="ECO:0007829|PDB:1AOH"
FT STRAND 1303..1305
FT /evidence="ECO:0007829|PDB:1AOH"
FT STRAND 1311..1322
FT /evidence="ECO:0007829|PDB:1AOH"
FT STRAND 1328..1342
FT /evidence="ECO:0007829|PDB:1AOH"
FT STRAND 1351..1354
FT /evidence="ECO:0007829|PDB:1AOH"
FT STRAND 1356..1360
FT /evidence="ECO:0007829|PDB:1AOH"
FT STRAND 1550..1553
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1555..1558
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1563..1572
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1580..1586
FT /evidence="ECO:0007829|PDB:3KCP"
FT TURN 1589..1591
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1592..1599
FT /evidence="ECO:0007829|PDB:3KCP"
FT HELIX 1608..1610
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1612..1617
FT /evidence="ECO:0007829|PDB:3KCP"
FT HELIX 1618..1620
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1622..1628
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1632..1634
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1642..1651
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1658..1671
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1681..1683
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1685..1689
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1696..1708
FT /evidence="ECO:0007829|PDB:3KCP"
FT TURN 1712..1714
FT /evidence="ECO:0007829|PDB:3KCP"
FT HELIX 1715..1719
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1723..1726
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1732..1734
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1739..1746
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1749..1758
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1761..1763
FT /evidence="ECO:0007829|PDB:5G5D"
FT STRAND 1765..1774
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1781..1783
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1785..1787
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1789..1791
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1793..1797
FT /evidence="ECO:0007829|PDB:3KCP"
FT HELIX 1800..1807
FT /evidence="ECO:0007829|PDB:3KCP"
FT TURN 1808..1811
FT /evidence="ECO:0007829|PDB:3KCP"
FT HELIX 1821..1823
FT /evidence="ECO:0007829|PDB:3KCP"
FT STRAND 1824..1826
FT /evidence="ECO:0007829|PDB:5G5D"
FT STRAND 1828..1830
FT /evidence="ECO:0007829|PDB:3KCP"
FT HELIX 1833..1840
FT /evidence="ECO:0007829|PDB:3KCP"
FT TURN 1841..1844
FT /evidence="ECO:0007829|PDB:3KCP"
FT HELIX 1847..1849
FT /evidence="ECO:0007829|PDB:3KCP"
SQ SEQUENCE 1853 AA; 196833 MW; 3ABDDC03ABFC5372 CRC64;
MRKVISMLLV VAMLTTIFAA MIPQTVSAAT MTVEIGKVTA AVGSKVEIPI TLKGVPSKGM
ANCDFVLGYD PNVLEVTEVK PGSIIKDPDP SKSFDSAIYP DRKMIVFLFA EDSGRGTYAI
TQDGVFATIV ATVKSAAAAP ITLLEVGAFA DNDLVEISTT FVAGGVNLGS SVPTTQPNVP
SDGVVVEIGK VTGSVGTTVE IPVYFRGVPS KGIANCDFVF RYDPNVLEII GIDPGDIIVD
PNPTKSFDTA IYPDRKIIVF LFAEDSGTGA YAITKDGVFA KIRATVKSSA PGYITFDEVG
GFADNDLVEQ KVSFIDGGVN VGNATPTKGA TPTNTATPTK SATATPTRPS VPTNTPTNTP
ANTPVSGNLK VEFYNSNPSD TTNSINPQFK VTNTGSSAID LSKLTLRYYY TVDGQKDQTF
WCDHAAIIGS NGSYNGITSN VKGTFVKMSS STNNADTYLE ISFTGGTLEP GAHVQIQGRF
AKNDWSNYTQ SNDYSFKSAS QFVEWDQVTA YLNGVLVWGK EPGGSVVPST QPVTTPPATT
KPPATTKPPA TTIPPSDDPN AIKIKVDTVN AKPGDTVNIP VRFSGIPSKG IANCDFVYSY
DPNVLEIIEI KPGELIVDPN PDKSFDTAVY PDRKIIVFLF AEDSGTGAYA ITKDGVFATI
VAKVKSGAPN GLSVIKFVEV GGFANNDLVE QRTQFFDGGV NVGDTTVPTT PTTPVTTPTD
DSNAVRIKVD TVNAKPGDTV RIPVRFSGIP SKGIANCDFV YSYDPNVLEI IEIEPGDIIV
DPNPDKSFDT AVYPDRKIIV FLFAEDSGTG AYAITKDGVF ATIVAKVKSG APNGLSVIKF
VEVGGFANND LVEQKTQFFD GGVNVGDTTE PATPTTPVTT PTTTDDLDAV RIKVDTVNAK
PGDTVRIPVR FSGIPSKGIA NCDFVYSYDP NVLEIIEIEP GDIIVDPNPD KSFDTAVYPD
RKIIVFLFAE DSGTGAYAIT KDGVFATIVA KVKSGAPNGL SVIKFVEVGG FANNDLVEQK
TQFFDGGVNV GDTTEPATPT TPVTTPTTTD DLDAVRIKVD TVNAKPGDTV RIPVRFSGIP
SKGIANCDFV YSYDPNVLEI IEIEPGDIIV DPNPDKSFDT AVYPDRKIIV FLFAEDSGTG
AYAITKDGVF ATIVAKVKEG APNGLSVIKF VEVGGFANND LVEQKTQFFD GGVNVGDTTE
PATPTTPVTT PTTTDDLDAV RIKVDTVNAK PGDTVRIPVR FSGIPSKGIA NCDFVYSYDP
NVLEIIEIEP GELIVDPNPT KSFDTAVYPD RKMIVFLFAE DSGTGAYAIT EDGVFATIVA
KVKSGAPNGL SVIKFVEVGG FANNDLVEQK TQFFDGGVNV GDTTEPATPT TPVTTPTTTD
DLDAVRIKVD TVNAKPGDTV RIPVRFSGIP SKGIANCDFV YSYDPNVLEI IEIEPGDIIV
DPNPDKSFDT AVYPDRKIIV FLFAEDSGTG AYAITKDGVF ATIVAKVKEG APNGLSVIKF
VEVGGFANND LVEQKTQFFD GGVNVGDTTV PTTSPTTTPP EPTITPNKLT LKIGRAEGRP
GDTVEIPVNL YGVPQKGIAS GDFVVSYDPN VLEIIEIEPG ELIVDPNPTK SFDTAVYPDR
KMIVFLFAED SGTGAYAITE DGVFATIVAK VKEGAPEGFS AIEISEFGAF ADNDLVEVET
DLINGGVLVT NKPVIEGYKV SGYILPDFSF DATVAPLVKA GFKVEIVGTE LYAVTDANGY
FEITGVPANA SGYTLKISRA TYLDRVIANV VVTGDTSVST SQAPIMMWVG DIVKDNSINL
LDVAEVIRCF NATKGSANYV EELDINRNGA INMQDIMIVH KHFGATSSDY DAQ
