Unreviewed, UniProtKB/TrEMBL Q45996 (Q45996_9CLOT)

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
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	peptidoglycan-based cell wall Inferred from electronic annotation. Source: InterPro
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro
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

Sequences

	Sequence		Length	Mass (Da)
	Q45996-1 [UniParc]. Last modified March 1, 2001. Version 3. Checksum: F8651504EC27809F	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

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 (2.0 ANGSTROMS) OF 287-428.
[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 (2.2 ANGSTROMS) OF 28-187.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U40345 Genomic DNA. Translation: AAC28899.2.

PIR

PC6006.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein family/group databases

CAZy

CBM3. Carbohydrate-Binding Module Family 3.

Family and domain databases

InterPro

IPR001956. CBD_3.
IPR002102. Cohesin.
IPR018452. Cohesin_region_subgroup.
IPR005102. DUF291.
IPR006162. Ppantne_S.
[Graphical view]

Gene3D

G3DSA:2.60.40.710. CBD_3. 1 hit.
G3DSA:2.60.40.680. Cohesin. 8 hits.

Pfam

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

ProDom

PD001947. CBD_3. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS51172. CBM3. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 7 hits. Uncertain.
[Graphical view]

ProtoNet

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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:	June 16, 2009
This is version 45 of the entry and version 3 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)