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Reviewed, UniProtKB/Swiss-Prot Q06851 (CIPA_CLOTH)

Last modified June 16, 2009. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Cellulosomal-scaffolding protein A
Alternative name(s):
    Cellulosomal glycoprotein S1/SL
    Cellulose-integrating protein A
    Cohesin
Gene names
Name: cipA
Ordered Locus Names: Cthe_3077
OrganismClostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]
Taxonomic identifier203119 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

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Protein attributes

Sequence length1853 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Acts as a scaffolding protein in the cellulosome. It promotes binding of cellulose to the catalytic domains of the cellulolytic enzymes.

Subcellular location

Secreted. Note: Remains at the cell surface.

Domain

The cohesin domains bind to the dockerin domain born by the catalytic components of the cellulosome.

Post-translational modification

O-glycosylated on most but not all Thr residues of the linker units. The reducing sugar is galactopyranose. Ref.4

Sequence similarities

Contains 1 CBM3 (carbohydrate binding type-3) domain.

Contains 9 cohesin domains.

Contains 2 dockerin domains.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

xynYP515841EBI-687595,EBI-1037473From a different organism.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.1
Chain29 – 18531825Cellulosomal-scaffolding protein A
PRO_0000020932

Regions

Domain29 – 182154Cohesin 1
Domain183 – 322140Cohesin 2
Domain365 – 523159CBM3
Domain560 – 704145Cohesin 3
Domain724 – 866143Cohesin 4
Domain889 – 1031143Cohesin 5
Domain1054 – 1196143Cohesin 6
Domain1219 – 1361143Cohesin 7
Domain1384 – 1526143Cohesin 8
Domain1548 – 1690143Cohesin 9
Domain1791 – 181424Dockerin 1
Domain1824 – 184724Dockerin 2
Region323 – 36341Linker (Pro/Thr-rich)
Region523 – 55937Linker (Pro/Thr-rich)

Experimental info

Sequence conflict16151A → AA AA sequence Ref.1

Secondary structure

1 .................................................................................................................. 1853
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q06851-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 3ABDDC03ABFC5372

FASTA1,853196,833
        10         20         30         40         50         60 
MRKVISMLLV VAMLTTIFAA MIPQTVSAAT MTVEIGKVTA AVGSKVEIPI TLKGVPSKGM 

        70         80         90        100        110        120 
ANCDFVLGYD PNVLEVTEVK PGSIIKDPDP SKSFDSAIYP DRKMIVFLFA EDSGRGTYAI 

       130        140        150        160        170        180 
TQDGVFATIV ATVKSAAAAP ITLLEVGAFA DNDLVEISTT FVAGGVNLGS SVPTTQPNVP 

       190        200        210        220        230        240 
SDGVVVEIGK VTGSVGTTVE IPVYFRGVPS KGIANCDFVF RYDPNVLEII GIDPGDIIVD 

       250        260        270        280        290        300 
PNPTKSFDTA IYPDRKIIVF LFAEDSGTGA YAITKDGVFA KIRATVKSSA PGYITFDEVG 

       310        320        330        340        350        360 
GFADNDLVEQ KVSFIDGGVN VGNATPTKGA TPTNTATPTK SATATPTRPS VPTNTPTNTP 

       370        380        390        400        410        420 
ANTPVSGNLK VEFYNSNPSD TTNSINPQFK VTNTGSSAID LSKLTLRYYY TVDGQKDQTF 

       430        440        450        460        470        480 
WCDHAAIIGS NGSYNGITSN VKGTFVKMSS STNNADTYLE ISFTGGTLEP GAHVQIQGRF 

       490        500        510        520        530        540 
AKNDWSNYTQ SNDYSFKSAS QFVEWDQVTA YLNGVLVWGK EPGGSVVPST QPVTTPPATT 

       550        560        570        580        590        600 
KPPATTKPPA TTIPPSDDPN AIKIKVDTVN AKPGDTVNIP VRFSGIPSKG IANCDFVYSY 

       610        620        630        640        650        660 
DPNVLEIIEI KPGELIVDPN PDKSFDTAVY PDRKIIVFLF AEDSGTGAYA ITKDGVFATI 

       670        680        690        700        710        720 
VAKVKSGAPN GLSVIKFVEV GGFANNDLVE QRTQFFDGGV NVGDTTVPTT PTTPVTTPTD 

       730        740        750        760        770        780 
DSNAVRIKVD TVNAKPGDTV RIPVRFSGIP SKGIANCDFV YSYDPNVLEI IEIEPGDIIV 

       790        800        810        820        830        840 
DPNPDKSFDT AVYPDRKIIV FLFAEDSGTG AYAITKDGVF ATIVAKVKSG APNGLSVIKF 

       850        860        870        880        890        900 
VEVGGFANND LVEQKTQFFD GGVNVGDTTE PATPTTPVTT PTTTDDLDAV RIKVDTVNAK 

       910        920        930        940        950        960 
PGDTVRIPVR FSGIPSKGIA NCDFVYSYDP NVLEIIEIEP GDIIVDPNPD KSFDTAVYPD 

       970        980        990       1000       1010       1020 
RKIIVFLFAE DSGTGAYAIT KDGVFATIVA KVKSGAPNGL SVIKFVEVGG FANNDLVEQK 

      1030       1040       1050       1060       1070       1080 
TQFFDGGVNV GDTTEPATPT TPVTTPTTTD DLDAVRIKVD TVNAKPGDTV RIPVRFSGIP 

      1090       1100       1110       1120       1130       1140 
SKGIANCDFV YSYDPNVLEI IEIEPGDIIV DPNPDKSFDT AVYPDRKIIV FLFAEDSGTG 

      1150       1160       1170       1180       1190       1200 
AYAITKDGVF ATIVAKVKEG APNGLSVIKF VEVGGFANND LVEQKTQFFD GGVNVGDTTE 

      1210       1220       1230       1240       1250       1260 
PATPTTPVTT PTTTDDLDAV RIKVDTVNAK PGDTVRIPVR FSGIPSKGIA NCDFVYSYDP 

      1270       1280       1290       1300       1310       1320 
NVLEIIEIEP GELIVDPNPT KSFDTAVYPD RKMIVFLFAE DSGTGAYAIT EDGVFATIVA 

      1330       1340       1350       1360       1370       1380 
KVKSGAPNGL SVIKFVEVGG FANNDLVEQK TQFFDGGVNV GDTTEPATPT TPVTTPTTTD 

      1390       1400       1410       1420       1430       1440 
DLDAVRIKVD TVNAKPGDTV RIPVRFSGIP SKGIANCDFV YSYDPNVLEI IEIEPGDIIV 

      1450       1460       1470       1480       1490       1500 
DPNPDKSFDT AVYPDRKIIV FLFAEDSGTG AYAITKDGVF ATIVAKVKEG APNGLSVIKF 

      1510       1520       1530       1540       1550       1560 
VEVGGFANND LVEQKTQFFD GGVNVGDTTV PTTSPTTTPP EPTITPNKLT LKIGRAEGRP 

      1570       1580       1590       1600       1610       1620 
GDTVEIPVNL YGVPQKGIAS GDFVVSYDPN VLEIIEIEPG ELIVDPNPTK SFDTAVYPDR 

      1630       1640       1650       1660       1670       1680 
KMIVFLFAED SGTGAYAITE DGVFATIVAK VKEGAPEGFS AIEISEFGAF ADNDLVEVET 

      1690       1700       1710       1720       1730       1740 
DLINGGVLVT NKPVIEGYKV SGYILPDFSF DATVAPLVKA GFKVEIVGTE LYAVTDANGY 

      1750       1760       1770       1780       1790       1800 
FEITGVPANA SGYTLKISRA TYLDRVIANV VVTGDTSVST SQAPIMMWVG DIVKDNSINL 

      1810       1820       1830       1840       1850 
LDVAEVIRCF NATKGSANYV EELDINRNGA INMQDIMIVH KHFGATSSDY DAQ

« Hide

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References

« Hide 'large scale' references
[1]"Sequencing of a Clostridium thermocellum gene (cipA) encoding the cellulosomal SL-protein reveals an unusual degree of internal homology."
Gerngross U.T., Romaniec M.P.M., Kobayashi T., Huskisson N.S., Demain A.L.
Mol. Microbiol. 8:325-334(1993) [PubMed: 8316083] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-40 AND 42-43.
[2]"Complete sequence of Clostridium thermocellum ATCC 27405."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Organization of a Clostridium thermocellum gene cluster encoding the cellulosomal scaffolding protein CipA and a protein possibly involved in attachment of the cellulosome to the cell surface."
Fujino T., Beguin P., Aubert J.-P.
J. Bacteriol. 175:1891-1899(1993) [PubMed: 8458832] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1820-1853.
[4]"The nature of the carbohydrate-peptide linkage region in glycoproteins from the cellulosomes of Clostridium thermocellum and Bacteroides cellulosolvens."
Gerwig G.J., Kamerling J.P., Vliegenthart J.F.G., Morag E., Lamed R., Bayer E.A.
J. Biol. Chem. 268:26956-26960(1993) [PubMed: 8262930] [Abstract]
Cited for: GLYCOSYLATION.
Strain: YS.
[5]"A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly."
Shimon L.J.W., Bayer E.A., Morag E., Lamed R., Yaron S., Shoham Y., Frolow F.
Structure 5:381-390(1997) [PubMed: 9083107] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 184-321.
[6]"Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose."
Tormo J., Lamed R., Chirino A.J., Morag E., Bayer E.A., Shoham Y., Steitz T.A.
EMBO J. 15:5739-5751(1996) [PubMed: 8918451] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 368-522.
[7]"The crystal structure of a type I cohesin domain at 1.7-A resolution."
Tavares G.A., Beguin P., Alzari P.M.
J. Mol. Biol. 273:701-713(1997) [PubMed: 9402065] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1213-1361.
+Additional computationally mapped references.

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Cross-references

Sequence databases

L08665 Genomic DNA. No translation available.
CP000568 Genomic DNA. Translation: ABN54273.1.
X67506 Genomic DNA. Translation: CAA47840.1.
PIRS36859.
RefSeqYP_001039466.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1ANUX-ray2.15A184-321[»]
1AOHX-ray1.70A/B1216-1361[»]
1NBCX-ray1.75A/B368-522[»]
1OHZX-ray2.20A181-340[»]
2B59X-ray2.11B1691-1853[»]
2CCLX-ray2.03A/C181-328[»]
SMRQ06851. Positions 558-703, 721-866, 886-1031, 1051-1196, 1551-1689.
ModBaseSearch...

Protein-protein interaction databases

IntActQ06851. 12 interactions.

Protein family/group databases

CAZyCBM3. Carbohydrate-Binding Module Family 3.

Genome annotation databases

GeneID4809951.
GenomeReviewsGene locus Cthe_3077 in contig CP000568_GR.
KEGGcth:Cthe_3077.
NMPDRfig|203119.1.peg.304.

Organism-specific databases

CMRSearch...

Family and domain databases

InterProIPR001956. CBD_3.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR002102. Cohesin.
IPR018452. Cohesin_region_subgroup.
IPR018247. EF_HAND_1.
[Graphical view]
Gene3DG3DSA:2.60.40.710. CBD_3. 1 hit.
G3DSA:2.60.40.680. Cohesin. 9 hits.
PfamPF00942. CBM_3. 1 hit.
PF00963. Cohesin. 9 hits.
[Graphical view]
ProDomPD001947. CBD_3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS51172. CBM3. 1 hit.
PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 1 hit. Uncertain.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCIPA_CLOTH
AccessionPrimary (citable) accession number: Q06851
Secondary accession number(s): A3DJZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents