Scaffolding protein precursor - Clostridium cellulolyticum

Preferred order of sections

Names and origin

Protein names

Submitted name:
Scaffolding protein EMBL AAC28899.2

Gene names

Name:

cipC EMBL AAC28899.2

Organism

Clostridium cellulolyticum EMBL AAC28899.2

Taxonomic identifier

1521 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	1546 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

Ontologies

Keywords
Domain	Signal EMBL AAC28899.2
Ligand	Calcium PDB 1G43 Metal-binding PDB 1G43
Technical term	3D-structure PDB 2VN5 PDB 1G1K PDB 1EHX PDB 1G43 PDB 2VN6
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Potential EMBL AAC28899.2

Chain

28 – 1546

1519

scaffolding protein EMBL AAC28899.2

PRO_5000144790

Sites

Metal binding

75

1

Calcium PDB 1G43

Metal binding

77

1

Calcium PDB 1G43

Metal binding

154

1

Calcium; via carbonyl oxygen PDB 1G43

Metal binding

157

1

Calcium PDB 1G43

Metal binding

158

1

Calcium PDB 1G43

Sequences

Sequence

Length

Mass (Da)

Tools

Q45996 [UniParc].

Last modified March 1, 2001. Version 3.
Checksum: F8651504EC27809F
Show »

FASTA

1,546

158,749

        10         20         30         40         50         60 
MRKKSLAFLL ALTMLVTLLG AQLTAFAAGT GVVSVQFNNG SSPASSNSIY ARFKVTNTSG 

        70         80         90        100        110        120 
SPINLADLKL RYYYTQDADK PLTFWCDHAG YMSGSNYIDA TSKVTGSFKA VSPAVTNADH 

       130        140        150        160        170        180 
YLEVALNSDA GSLPAGGSIE IQTRFARNDW SNFDQSNDWS YTAAGSYMDW QKISAFVGGT 

       190        200        210        220        230        240 
LAYGSTPDGG NPPPQDPTIN PTSISAKAGS FADTKITLTP NGNTFNGISE LQSSQYTKGT 

       250        260        270        280        290        300 
NEVTLLASYL NTLPENTTKT LTFDFGVGTK NPKLTITVLP KDIPGDSLKV TVGTANGKPG 

       310        320        330        340        350        360 
DTVTVPVTFA DVAKMKNVGT CNFYLGYDAS LLEVVSVDAG PIVKNAAVNF SSSASNGTIS 

       370        380        390        400        410        420 
FLFLDNTITD ELITADGVFA NIKFKLKSVT AKTTTPVTFK DGGAFGDGTM SKIASVTKTN 

       430        440        450        460        470        480 
GSVTIDPGTQ PTKELKVAVG TANGKPGDTV TVPVTFADVV NVGNVGTCNF YLAYDASLLE 

       490        500        510        520        530        540 
VVSVDAGPIV KNAAVNFSSS ASNGTISFLF LDNTITDELI TSDGVFANIK FKLKSVATKT 

       550        560        570        580        590        600 
TTPVTFKDGG AFGDGTMAKI ATVTKTNGSV TIDPGTQPTK ELKVAVGTAN GKPGDTVTVP 

       610        620        630        640        650        660 
VTFADVASAG NVGTCNFYLA YDASLLEVVS VDAGPIVKNA AVNFSSSASN GSISFLFLDN 

       670        680        690        700        710        720 
TITDELITAD GVFANIKFKL KSVAAKTTTP VTFKDGGAFG DGTMTKIATV TKTNGSVTID 

       730        740        750        760        770        780 
PGTQPTKELK VAVGTAEGNV GDTVTVPVTF ADVASAGNVG TCNFYLAYDA SLLDVVSVAA 

       790        800        810        820        830        840 
GPIVKNAAVN FSSSASNGSI SFLFLDNTIT DELITADGVF ANITFKLKSV TAKTTTPVTF 

       850        860        870        880        890        900 
KDGGAFGDGT MAKIATVTKT NGSVTIVPGI QPTKELKVAV GTAEGNVGDT VTVPVTFADV 

       910        920        930        940        950        960 
ASAGNVGTCN FYLAYDASLL DVVSVAAGPI VKNAAVNFSS SASNGSISFL FLDNTITDEL 

       970        980        990       1000       1010       1020 
ITADGVFANI SFKLKSVTSK TTTPVTFKDG GAFGDGTMAK IATVIKTNGS VTIVPGIQPT 

      1030       1040       1050       1060       1070       1080 
KELKVAVGTA EGNVGDTVTV PVTFADVASA GNVGTCNFYL AYDASLLDVV SHAAGPIVKN 

      1090       1100       1110       1120       1130       1140 
RAVNFSSSAS NGSISFLFLD NTITDELITA DGVFANITFK LKSVAAKTTT PVTFKDGGAF 

      1150       1160       1170       1180       1190       1200 
GDGTMAKIAT VTKTNGSVTI VPGIQPTKEL KVAVGTASGK AGDTVTVPVT FADVATVGNV 

      1210       1220       1230       1240       1250       1260 
GTCNFYVTYD TNLLEVASVT PGSIVTNAAV NFSSSTSNGT ISFLFLDNTI TDQLIKTDGT 

      1270       1280       1290       1300       1310       1320 
FAEIKFKLKS VTAKTTTPVA FKDGGAFGDG TMAKIATVTK TNGSVTIDVG DVTPVNPTIT 

      1330       1340       1350       1360       1370       1380 
PSTASFDKYV PANVNVTLTP NGNTFKGITG LTSGTDFTVS NNVVTISKSY LSTLAVGSKT 

      1390       1400       1410       1420       1430       1440 
LTFDFGVTNN PVLTLTITDS TPVVTGLGVK IASVTGKTGD TITVPVTLSN VVKSGNVGTC 

      1450       1460       1470       1480       1490       1500 
NFYITYDASM LQAVSATAGD IVLNAPVNFS SSINATTGTI SILFLDNTIG DQLITSDGVV 

      1510       1520       1530       1540 
ANLTFKVVGT SSTTTPIAFK AGGAFGNGNM SKISDITFTN GSAKLN

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References

[1]	"Interaction between the endoglucanase CelA and the scaffolding protein CipC of the Clostridium cellulolyticum cellulosome." Pages S., Belaich A., Tardif C., Reverbel-Leroy C., Gaudin C., Belaich J.P. J. Bacteriol. 178:2279-2286(1996) [PubMed: 8636029] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 35319 EMBL AAC28899.2.
[2]	"Sequence analysis of scaffolding protein CipC and ORFXp, a new cohesin-containing protein in Clostridium cellulolyticum: comparison of various cohesin domains and subcellular localization of ORFXp." Pages S., Belaich A., Fierobe H.P., Tardif C., Gaudin C., Belaich J.P. J. Bacteriol. 181:1801-1810(1999) [PubMed: 10074072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 35319 EMBL AAC28899.2.
[3]	"Molecular study and overexpression of the Clostridium cellulolyticum celCCF cellulase gene in Escherichia coli." Reverbel-Leroy C., Tardif C., Belaich A., Bernadac A., Gaudin C., Belaich J. Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 35319 EMBL AAC28899.2.
[4]	Pages S., Belaich A., Reverbel C., Tardif C., Fierobe H.P., Gaudin C., Belaich J.P. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 35319 EMBL AAC28899.2.
[5]	"Crystal structure of a cohesin module from Clostridium cellulolyticum: implications for dockerin recognition." Spinelli S., Fierobe H.P., Belaich A., Belaich J.P., Henrissat B., Cambillau C. J. Mol. Biol. 304:189-200(2000) [PubMed: 11080455] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 287-427.
[6]	"Solution structure of the module X2 1 of unknown function of the cellulosomal scaffolding protein CipC of Clostridium cellulolyticum." Mosbah A., Belaich A., Bornet O., Belaich J.P., Henrissat B., Darbon H. J. Mol. Biol. 304:201-217(2000) [PubMed: 11080456] [Abstract] Cited for: STRUCTURE BY NMR OF 195-285.
[7]	"Structure of a family IIIa scaffoldin CBD from the cellulosome of Clostridium cellulolyticum at 2.2 A resolution." Shimon L.J., Pages S., Belaich A., Belaich J.P., Bayer E.A., Lamed R., Shoham Y., Frolow F. Acta Crystallogr. D Biol. Crystallogr. 56:1560-1568(2000) [PubMed: 11092922] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 28-187 IN COMPLEX WITH CALCIUM.
[8]	"The Clostridium cellulolyticum dockerin displays a dual binding mode for its cohesin partner." Pinheiro B.A., Proctor M.R., Martinez-Fleites C., Prates J.A., Money V.A., Davies G.J., Bayer E.A., Fontesm C.M., Fierobe H.P., Gilbert H.J. J. Biol. Chem. 283:18422-18430(2008) [PubMed: 18445585] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 277-427.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U40345 Genomic DNA. Translation: AAC28899.2.

PIR

PC6006.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EHX	NMR	-	A	195-285	[»]
1G1K	X-ray	2.00	A/B	287-427	[»]
1G43	X-ray	2.20	A	28-187	[»]
2VN5	X-ray	1.90	A/C	277-427	[»]
2VN6	X-ray	1.49	A	277-427	[»]

ProteinModelPortal

Q45996.

SMR

Q45996. Positions 28-187, 195-1015, 1023-1163, 1170-1308, 1407-1546.

ModBase

Search...

Protein family/group databases

CAZy

CBM3. Carbohydrate-Binding Module Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR002102. Cohesin_dom.
IPR018452. Cohesin_dom_subgr.
IPR005102. DUF291.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]

Gene3D

G3DSA:2.60.40.710. CBD_3. 1 hit.
G3DSA:2.60.40.680. Cohesin. 8 hits.
G3DSA:2.60.40.10. Ig-like_fold. 2 hits.

Pfam

PF00942. CBM_3. 1 hit.
PF00963. Cohesin. 8 hits.
PF03442. DUF291. 2 hits.
[Graphical view]

SMART

SM01067. CBM_3. 1 hit.
[Graphical view]

SUPFAM

SSF49384. Cellul_bind. 9 hits.
SSF81296. Ig_E-set. 2 hits.

PROSITE

PS51172. CBM3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q45996_9CLOT

Accession

Primary (citable) accession number: Q45996

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 59 of the entry and version 3 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)