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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

BioCyciMetaCyc: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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 281 PublicationAdd BLAST28
ChainiPRO_000002093229 – 1853Cellulosomal-scaffolding protein AAdd BLAST1825

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 interactors.
MINTiMINT-1204636.
STRINGi203119.Cthe_3077.

Structurei

Secondary structure

11853
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi184 – 188Combined sources5
Beta strandi198 – 207Combined sources10
Beta strandi213 – 221Combined sources9
Turni224 – 226Combined sources3
Beta strandi227 – 234Combined sources8
Helixi243 – 245Combined sources3
Beta strandi247 – 252Combined sources6
Turni253 – 256Combined sources4
Beta strandi257 – 263Combined sources7
Beta strandi265 – 269Combined sources5
Beta strandi277 – 286Combined sources10
Beta strandi288 – 290Combined sources3
Beta strandi292 – 303Combined sources12
Beta strandi312 – 315Combined sources4
Beta strandi317 – 320Combined sources4
Beta strandi369 – 376Combined sources8
Beta strandi380 – 383Combined sources4
Beta strandi387 – 393Combined sources7
Beta strandi395 – 397Combined sources3
Helixi401 – 403Combined sources3
Beta strandi404 – 410Combined sources7
Beta strandi418 – 428Combined sources11
Beta strandi434 – 436Combined sources3
Helixi438 – 440Combined sources3
Beta strandi441 – 452Combined sources12
Beta strandi455 – 465Combined sources11
Beta strandi473 – 482Combined sources10
Beta strandi488 – 490Combined sources3
Beta strandi508 – 512Combined sources5
Beta strandi515 – 518Combined sources4
Beta strandi1220 – 1224Combined sources5
Beta strandi1226 – 1229Combined sources4
Beta strandi1234 – 1243Combined sources10
Beta strandi1249 – 1257Combined sources9
Turni1260 – 1262Combined sources3
Beta strandi1263 – 1270Combined sources8
Helixi1279 – 1282Combined sources4
Beta strandi1283 – 1288Combined sources6
Turni1289 – 1292Combined sources4
Beta strandi1293 – 1299Combined sources7
Beta strandi1303 – 1305Combined sources3
Beta strandi1311 – 1322Combined sources12
Beta strandi1328 – 1342Combined sources15
Beta strandi1351 – 1354Combined sources4
Beta strandi1356 – 1360Combined sources5
Beta strandi1550 – 1553Combined sources4
Beta strandi1555 – 1558Combined sources4
Beta strandi1563 – 1572Combined sources10
Beta strandi1580 – 1586Combined sources7
Turni1589 – 1591Combined sources3
Beta strandi1592 – 1599Combined sources8
Helixi1608 – 1610Combined sources3
Beta strandi1612 – 1617Combined sources6
Helixi1618 – 1620Combined sources3
Beta strandi1622 – 1628Combined sources7
Beta strandi1632 – 1634Combined sources3
Beta strandi1642 – 1651Combined sources10
Beta strandi1658 – 1671Combined sources14
Beta strandi1681 – 1683Combined sources3
Beta strandi1685 – 1689Combined sources5
Beta strandi1696 – 1708Combined sources13
Turni1712 – 1714Combined sources3
Helixi1715 – 1719Combined sources5
Beta strandi1723 – 1726Combined sources4
Beta strandi1732 – 1734Combined sources3
Beta strandi1739 – 1746Combined sources8
Beta strandi1749 – 1758Combined sources10
Beta strandi1765 – 1774Combined sources10
Beta strandi1781 – 1783Combined sources3
Beta strandi1785 – 1787Combined sources3
Beta strandi1789 – 1791Combined sources3
Beta strandi1793 – 1797Combined sources5
Helixi1800 – 1807Combined sources8
Turni1808 – 1811Combined sources4
Helixi1821 – 1823Combined sources3
Beta strandi1828 – 1830Combined sources3
Helixi1833 – 1840Combined sources8
Turni1841 – 1844Combined sources4
Helixi1847 – 1849Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06851.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 182Cohesin 1Add BLAST154
Domaini183 – 322Cohesin 2Add BLAST140
Domaini365 – 523CBM3PROSITE-ProRule annotationAdd BLAST159
Domaini560 – 704Cohesin 3Add BLAST145
Domaini724 – 866Cohesin 4Add BLAST143
Domaini889 – 1031Cohesin 5Add BLAST143
Domaini1054 – 1196Cohesin 6Add BLAST143
Domaini1219 – 1361Cohesin 7Add BLAST143
Domaini1384 – 1526Cohesin 8Add BLAST143
Domaini1548 – 1690Cohesin 9Add BLAST143
Domaini1785 – 1852DockerinPROSITE-ProRule annotationAdd BLAST68

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni323 – 363Linker (Pro/Thr-rich)Add BLAST41
Regioni523 – 559Linker (Pro/Thr-rich)Add BLAST37

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.
OrthoDBiPOG091H061W.

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)DescriptionActionsGraphical viewLength
Sequence conflicti1615A → AA AA sequence (PubMed:8316083).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-42322N.
IntActiQ06851. 12 interactors.
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.
OrthoDBiPOG091H061W.

Enzyme and pathway databases

BioCyciMetaCyc: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...

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: November 2, 2016
This is version 132 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.