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Protein

Cellulosomal-scaffolding protein A

Gene

cipA

Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciCTHE203119:GIW8-3190-MONOMER.
MetaCyc:MONOMER-16412.

Protein family/group databases

CAZyiCBM3. Carbohydrate-Binding Module Family 3.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellulosomal-scaffolding protein A
Alternative name(s):
Cellulose-integrating protein A
Cellulosomal glycoprotein S1/SL
Cohesin
Gene namesi
Name:cipA
Ordered Locus Names:Cthe_3077
OrganismiClostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
Taxonomic identifieri203119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
Proteomesi
  • UP000002145 Componenti: Chromosome

Subcellular locationi

  • Secreted

  • Note: Remains at the cell surface.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28281 PublicationAdd
BLAST
Chaini29 – 18531825Cellulosomal-scaffolding protein APRO_0000020932Add
BLAST

Post-translational modificationi

O-glycosylated on most but not all Thr residues of the linker units. The reducing sugar is galactopyranose.1 Publication

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

DIPiDIP-42322N.
IntActiQ06851. 12 interactions.
MINTiMINT-1204636.
STRINGi203119.Cthe_3077.

Structurei

Secondary structure

1
1853
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi184 – 1885Combined sources
Beta strandi198 – 20710Combined sources
Beta strandi213 – 2219Combined sources
Turni224 – 2263Combined sources
Beta strandi227 – 2348Combined sources
Helixi243 – 2453Combined sources
Beta strandi247 – 2526Combined sources
Turni253 – 2564Combined sources
Beta strandi257 – 2637Combined sources
Beta strandi265 – 2695Combined sources
Beta strandi277 – 28610Combined sources
Beta strandi288 – 2903Combined sources
Beta strandi292 – 30312Combined sources
Beta strandi312 – 3154Combined sources
Beta strandi317 – 3204Combined sources
Beta strandi369 – 3768Combined sources
Beta strandi380 – 3834Combined sources
Beta strandi387 – 3937Combined sources
Beta strandi395 – 3973Combined sources
Helixi401 – 4033Combined sources
Beta strandi404 – 4107Combined sources
Beta strandi418 – 42811Combined sources
Beta strandi434 – 4363Combined sources
Helixi438 – 4403Combined sources
Beta strandi441 – 45212Combined sources
Beta strandi455 – 46511Combined sources
Beta strandi473 – 48210Combined sources
Beta strandi488 – 4903Combined sources
Beta strandi508 – 5125Combined sources
Beta strandi515 – 5184Combined sources
Beta strandi1220 – 12245Combined sources
Beta strandi1226 – 12294Combined sources
Beta strandi1234 – 124310Combined sources
Beta strandi1249 – 12579Combined sources
Turni1260 – 12623Combined sources
Beta strandi1263 – 12708Combined sources
Helixi1279 – 12824Combined sources
Beta strandi1283 – 12886Combined sources
Turni1289 – 12924Combined sources
Beta strandi1293 – 12997Combined sources
Beta strandi1303 – 13053Combined sources
Beta strandi1311 – 132212Combined sources
Beta strandi1328 – 134215Combined sources
Beta strandi1351 – 13544Combined sources
Beta strandi1356 – 13605Combined sources
Beta strandi1550 – 15534Combined sources
Beta strandi1555 – 15584Combined sources
Beta strandi1563 – 157210Combined sources
Beta strandi1580 – 15867Combined sources
Turni1589 – 15913Combined sources
Beta strandi1592 – 15998Combined sources
Helixi1608 – 16103Combined sources
Beta strandi1612 – 16176Combined sources
Helixi1618 – 16203Combined sources
Beta strandi1622 – 16287Combined sources
Beta strandi1632 – 16343Combined sources
Beta strandi1642 – 165110Combined sources
Beta strandi1658 – 167114Combined sources
Beta strandi1681 – 16833Combined sources
Beta strandi1685 – 16895Combined sources
Beta strandi1696 – 170813Combined sources
Turni1712 – 17143Combined sources
Helixi1715 – 17195Combined sources
Beta strandi1723 – 17264Combined sources
Beta strandi1732 – 17343Combined sources
Beta strandi1739 – 17468Combined sources
Beta strandi1749 – 175810Combined sources
Beta strandi1765 – 177410Combined sources
Beta strandi1781 – 17833Combined sources
Beta strandi1785 – 17873Combined sources
Beta strandi1789 – 17913Combined sources
Beta strandi1793 – 17975Combined sources
Helixi1800 – 18078Combined sources
Turni1808 – 18114Combined sources
Helixi1821 – 18233Combined sources
Beta strandi1828 – 18303Combined sources
Helixi1833 – 18408Combined sources
Turni1841 – 18444Combined sources
Helixi1847 – 18493Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
3KCPX-ray1.94A1542-1853[»]
4B9FX-ray1.19A/B368-519[»]
ProteinModelPortaliQ06851.
SMRiQ06851. Positions 31-174, 183-328, 368-522, 558-703, 721-866, 886-1031, 1051-1196, 1216-1361, 1381-1526, 1551-1689, 1697-1852.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06851.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 182154Cohesin 1Add
BLAST
Domaini183 – 322140Cohesin 2Add
BLAST
Domaini365 – 523159CBM3PROSITE-ProRule annotationAdd
BLAST
Domaini560 – 704145Cohesin 3Add
BLAST
Domaini724 – 866143Cohesin 4Add
BLAST
Domaini889 – 1031143Cohesin 5Add
BLAST
Domaini1054 – 1196143Cohesin 6Add
BLAST
Domaini1219 – 1361143Cohesin 7Add
BLAST
Domaini1384 – 1526143Cohesin 8Add
BLAST
Domaini1548 – 1690143Cohesin 9Add
BLAST
Domaini1785 – 185268DockerinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni323 – 36341Linker (Pro/Thr-rich)Add
BLAST
Regioni523 – 55937Linker (Pro/Thr-rich)Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 CBM3 (carbohydrate binding type-3) domain.PROSITE-ProRule annotation
Contains 9 cohesin domains.Curated
Contains 1 dockerin domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG2730. LUCA.
OMAiSKGIANC.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
2.60.40.680. 9 hits.
2.60.40.710. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR008969. CarboxyPept-like_regulatory.
IPR001956. CBD_3.
IPR002102. Cohesin_dom.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR018247. EF_Hand_1_Ca_BS.
[Graphical view]
PfamiPF00942. CBM_3. 1 hit.
PF00963. Cohesin. 9 hits.
[Graphical view]
SMARTiSM01067. CBM_3. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 10 hits.
SSF49464. SSF49464. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS51172. CBM3. 1 hit.
PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS51766. DOCKERIN. 1 hit.
PS00018. EF_HAND_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q06851-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKVISMLLV VAMLTTIFAA MIPQTVSAAT MTVEIGKVTA AVGSKVEIPI
60 70 80 90 100
TLKGVPSKGM ANCDFVLGYD PNVLEVTEVK PGSIIKDPDP SKSFDSAIYP
110 120 130 140 150
DRKMIVFLFA EDSGRGTYAI TQDGVFATIV ATVKSAAAAP ITLLEVGAFA
160 170 180 190 200
DNDLVEISTT FVAGGVNLGS SVPTTQPNVP SDGVVVEIGK VTGSVGTTVE
210 220 230 240 250
IPVYFRGVPS KGIANCDFVF RYDPNVLEII GIDPGDIIVD PNPTKSFDTA
260 270 280 290 300
IYPDRKIIVF LFAEDSGTGA YAITKDGVFA KIRATVKSSA PGYITFDEVG
310 320 330 340 350
GFADNDLVEQ KVSFIDGGVN VGNATPTKGA TPTNTATPTK SATATPTRPS
360 370 380 390 400
VPTNTPTNTP ANTPVSGNLK VEFYNSNPSD TTNSINPQFK VTNTGSSAID
410 420 430 440 450
LSKLTLRYYY TVDGQKDQTF WCDHAAIIGS NGSYNGITSN VKGTFVKMSS
460 470 480 490 500
STNNADTYLE ISFTGGTLEP GAHVQIQGRF AKNDWSNYTQ SNDYSFKSAS
510 520 530 540 550
QFVEWDQVTA YLNGVLVWGK EPGGSVVPST QPVTTPPATT KPPATTKPPA
560 570 580 590 600
TTIPPSDDPN AIKIKVDTVN AKPGDTVNIP VRFSGIPSKG IANCDFVYSY
610 620 630 640 650
DPNVLEIIEI KPGELIVDPN PDKSFDTAVY PDRKIIVFLF AEDSGTGAYA
660 670 680 690 700
ITKDGVFATI VAKVKSGAPN GLSVIKFVEV GGFANNDLVE QRTQFFDGGV
710 720 730 740 750
NVGDTTVPTT PTTPVTTPTD DSNAVRIKVD TVNAKPGDTV RIPVRFSGIP
760 770 780 790 800
SKGIANCDFV YSYDPNVLEI IEIEPGDIIV DPNPDKSFDT AVYPDRKIIV
810 820 830 840 850
FLFAEDSGTG AYAITKDGVF ATIVAKVKSG APNGLSVIKF VEVGGFANND
860 870 880 890 900
LVEQKTQFFD GGVNVGDTTE PATPTTPVTT PTTTDDLDAV RIKVDTVNAK
910 920 930 940 950
PGDTVRIPVR FSGIPSKGIA NCDFVYSYDP NVLEIIEIEP GDIIVDPNPD
960 970 980 990 1000
KSFDTAVYPD RKIIVFLFAE DSGTGAYAIT KDGVFATIVA KVKSGAPNGL
1010 1020 1030 1040 1050
SVIKFVEVGG FANNDLVEQK TQFFDGGVNV GDTTEPATPT TPVTTPTTTD
1060 1070 1080 1090 1100
DLDAVRIKVD TVNAKPGDTV RIPVRFSGIP SKGIANCDFV YSYDPNVLEI
1110 1120 1130 1140 1150
IEIEPGDIIV DPNPDKSFDT AVYPDRKIIV FLFAEDSGTG AYAITKDGVF
1160 1170 1180 1190 1200
ATIVAKVKEG APNGLSVIKF VEVGGFANND LVEQKTQFFD GGVNVGDTTE
1210 1220 1230 1240 1250
PATPTTPVTT PTTTDDLDAV RIKVDTVNAK PGDTVRIPVR FSGIPSKGIA
1260 1270 1280 1290 1300
NCDFVYSYDP NVLEIIEIEP GELIVDPNPT KSFDTAVYPD RKMIVFLFAE
1310 1320 1330 1340 1350
DSGTGAYAIT EDGVFATIVA KVKSGAPNGL SVIKFVEVGG FANNDLVEQK
1360 1370 1380 1390 1400
TQFFDGGVNV GDTTEPATPT TPVTTPTTTD DLDAVRIKVD TVNAKPGDTV
1410 1420 1430 1440 1450
RIPVRFSGIP SKGIANCDFV YSYDPNVLEI IEIEPGDIIV DPNPDKSFDT
1460 1470 1480 1490 1500
AVYPDRKIIV FLFAEDSGTG AYAITKDGVF ATIVAKVKEG APNGLSVIKF
1510 1520 1530 1540 1550
VEVGGFANND LVEQKTQFFD GGVNVGDTTV PTTSPTTTPP EPTITPNKLT
1560 1570 1580 1590 1600
LKIGRAEGRP GDTVEIPVNL YGVPQKGIAS GDFVVSYDPN VLEIIEIEPG
1610 1620 1630 1640 1650
ELIVDPNPTK SFDTAVYPDR KMIVFLFAED SGTGAYAITE DGVFATIVAK
1660 1670 1680 1690 1700
VKEGAPEGFS AIEISEFGAF ADNDLVEVET DLINGGVLVT NKPVIEGYKV
1710 1720 1730 1740 1750
SGYILPDFSF DATVAPLVKA GFKVEIVGTE LYAVTDANGY FEITGVPANA
1760 1770 1780 1790 1800
SGYTLKISRA TYLDRVIANV VVTGDTSVST SQAPIMMWVG DIVKDNSINL
1810 1820 1830 1840 1850
LDVAEVIRCF NATKGSANYV EELDINRNGA INMQDIMIVH KHFGATSSDY

DAQ
Length:1,853
Mass (Da):196,833
Last modified:November 1, 1997 - v2
Checksum:i3ABDDC03ABFC5372
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1615 – 16151A → AA AA sequence (PubMed:8316083).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08665 Genomic DNA. No translation available.
CP000568 Genomic DNA. Translation: ABN54273.1.
X67506 Genomic DNA. Translation: CAA47840.1.
PIRiS36859.
RefSeqiWP_020458017.1. NC_009012.1.

Genome annotation databases

EnsemblBacteriaiABN54273; ABN54273; Cthe_3077.
KEGGicth:Cthe_3077.
PATRICi19520284. VBICloThe47081_3289.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08665 Genomic DNA. No translation available.
CP000568 Genomic DNA. Translation: ABN54273.1.
X67506 Genomic DNA. Translation: CAA47840.1.
PIRiS36859.
RefSeqiWP_020458017.1. NC_009012.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
3KCPX-ray1.94A1542-1853[»]
4B9FX-ray1.19A/B368-519[»]
ProteinModelPortaliQ06851.
SMRiQ06851. Positions 31-174, 183-328, 368-522, 558-703, 721-866, 886-1031, 1051-1196, 1216-1361, 1381-1526, 1551-1689, 1697-1852.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-42322N.
IntActiQ06851. 12 interactions.
MINTiMINT-1204636.
STRINGi203119.Cthe_3077.

Protein family/group databases

CAZyiCBM3. Carbohydrate-Binding Module Family 3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN54273; ABN54273; Cthe_3077.
KEGGicth:Cthe_3077.
PATRICi19520284. VBICloThe47081_3289.

Phylogenomic databases

eggNOGiCOG2730. LUCA.
OMAiSKGIANC.

Enzyme and pathway databases

BioCyciCTHE203119:GIW8-3190-MONOMER.
MetaCyc:MONOMER-16412.

Miscellaneous databases

EvolutionaryTraceiQ06851.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
2.60.40.680. 9 hits.
2.60.40.710. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR008969. CarboxyPept-like_regulatory.
IPR001956. CBD_3.
IPR002102. Cohesin_dom.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR018247. EF_Hand_1_Ca_BS.
[Graphical view]
PfamiPF00942. CBM_3. 1 hit.
PF00963. Cohesin. 9 hits.
[Graphical view]
SMARTiSM01067. CBM_3. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 10 hits.
SSF49464. SSF49464. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS51172. CBM3. 1 hit.
PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS51766. DOCKERIN. 1 hit.
PS00018. EF_HAND_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-40 AND 42-43.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372.
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1213-1361.

Entry informationi

Entry nameiCIPA_CLOTH
AccessioniPrimary (citable) accession number: Q06851
Secondary accession number(s): A3DJZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.