Q9X721 (Q9X721_CLOHI) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Collagenase EMBL BAA77453.1

Gene names

Name:

colG EMBL BAA77453.1

Organism

Clostridium histolyticum EMBL BAA77453.1

Taxonomic identifier

1498 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	1118 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Domain	Collagen EMBL BAA77453.1
Technical term	3D-structure PDB 3JS7 PDB 3JQU PDB 2Y3U PDB 2Y50 PDB 2Y6I PDB 2Y72 PDB 4HPK
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular_component	collagen Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9X721 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 770CF3F60E4D4FD4	FASTA	1,118	126,242
	10 20 30 40 50 60 MKKNILKILM DSYSKESKIQ TVRRVTSVSL LAVYLTMNTS SLVLAKPIEN TNDTSIKNVE 70 80 90 100 110 120 KLRNAPNEEN SKKVEDSKND KVEHVKNIEE AKVEQVAPEV KSKSTLRSAS IANTNSEKYD 130 140 150 160 170 180 FEYLNGLSYT ELTNLIKNIK WNQINGLFNY STGSQKFFGD KNRVQAIINA LQESGRTYTA 190 200 210 220 230 240 NDMKGIETFT EVLRAGFYLG YYNDGLSYLN DRNFQDKCIP AMIAIQKNPN FKLGTAVQDE 250 260 270 280 290 300 VITSLGKLIG NASANAEVVN NCVPVLKQFR ENLNQYAPDY VKGTAVNELI KGIEFDFSGA 310 320 330 340 350 360 AYEKDVKTMP WYGKIDPFIN ELKALGLYGN ITSATEWASD VGIYYLSKFG LYSTNRNDIV 370 380 390 400 410 420 QSLEKAVDMY KYGKIAFVAM ERITWDYDGI GSNGKKVDHD KFLDDAEKHY LPKTYTFDNG 430 440 450 460 470 480 TFIIRAGDKV SEEKIKRLYW ASREVKSQFH RVVGNDKALE VGNADDVLTM KIFNSPEEYK 490 500 510 520 530 540 FNTNINGVST DNGGLYIEPR GTFYTYERTP QQSIFSLEEL FRHEYTHYLQ ARYLVDGLWG 550 560 570 580 590 600 QGPFYEKNRL TWFDEGTAEF FAGSTRTSGV LPRKSILGYL AKDKVDHRYS LKKTLNSGYD 610 620 630 640 650 660 DSDWMFYNYG FAVAHYLYEK DMPTFIKMNK AILNTDVKSY DEIIKKLSDD ANKNTEYQNH 670 680 690 700 710 720 IQELADKYQG AGIPLVSDDY LKDHGYKKAS EVYSEISKAA SLTNTSVTAE KSQYFNTFTL 730 740 750 760 770 780 RGTYTGETSK GEFKDWDEMS KKLDGTLESL AKNSWSGYKT LTAYFTNYRV TSDNKVQYDV 790 800 810 820 830 840 VFHGVLTDNA DISNNKAPIA KVTGPSTGAV GRNIEFSGKD SKDEDGKIVS YDWDFGDGAT 850 860 870 880 890 900 SRGKNSVHAY KKAGTYNVTL KVTDDKGATA TESFTIEIKN EDTTTPITKE MEPNDDIKEA 910 920 930 940 950 960 NGPIVEGVTV KGDLNGSDDA DTFYFDVKED GDVTIELPYS GSSNFTWLVY KEGDDQNHIA 970 980 990 1000 1010 1020 SGIDKNNSKV GTFKSTKGRH YVFIYKHDSA SNISYSLNIK GLGNEKLKEK ENNDSSDKAT 1030 1040 1050 1060 1070 1080 VIPNFNTTMQ GSLLGDDSRD YYSFEVKEEG EVNIELDKKD EFGVTWTLHP ESNINDRITY 1090 1100 1110 GQVDGNKVSN KVKLRPGKYY LLVYKYSGSG NYELRVNK

References

[1]	"Gene duplication and multiplicity of collagenases in Clostridium histolyticum." Matsushita O., Jung C.-M., Katayama S., Minami J., Takahashi Y., Okabe A. J. Bacteriol. 181:923-933(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: JCM 1403 EMBL BAA77453.1.
[2]	"Crystal structure of Clostridium histolyticum colg collagenase PKD domain 2 at 1.6 Angstrom resolution." Sakon J., Philominathan S.T.L., Gunn S., Matsushita O. Submitted (SEP-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 797-881.
[3]	"Crystal structure of Clostridium histolyticum colG collagenase polycystic kidney disease domain at 1.4 Angstrom resolution." Sakon J, Philominathan S.T.L., Matsushita O., Gunn S. Submitted (SEP-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 797-881.
[4]	"Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis." Eckhard U., Schonauer E., Nuss D., Brandstetter H. Nat. Struct. Mol. Biol. 18:1109-1114(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) OF 799-880.
[5]	"Structural comparison of ColH and ColG collagen-binding domains from Clostridium histolyticum." Bauer R., Wilson J.J., Philominathan S.T., Davis D., Matsushita O., Sakon J. J. Bacteriol. 195:318-327(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1006-1118 AND 1003-1118.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D87215 Genomic DNA. Translation: BAA77453.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Y3U	X-ray	2.55	A	119-880	[»]
2Y50	X-ray	2.80	A	119-880	[»]
2Y6I	X-ray	3.25	A	119-880	[»]
2Y72	X-ray	1.18	A/B	799-880	[»]
3JQU	X-ray	1.40	A/B	797-881	[»]
3JS7	X-ray	1.60	A/B	797-881	[»]
4HPK	X-ray	1.35	A	1006-1118	[»]
			B	1003-1118	[»]

ProteinModelPortal

Q9X721.

SMR

Q9X721. Positions 1005-1118.

ModBase

Search...

Protein family/group databases

Allergome

5989. Clo hi Collagenase.

MEROPS

M09.002.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.60.40.670. 1 hit.

InterPro

IPR007280. Peptidase_C_arc/bac.
IPR013661. Peptidase_M9_N_dom.
IPR002169. Peptidase_M9A/M9B.
IPR022409. PKD/Chitinase_dom.
IPR000601. PKD_dom.
[Graphical view]

Pfam

PF01752. Peptidase_M9. 1 hit.
PF08453. Peptidase_M9_N. 1 hit.
PF00801. PKD. 1 hit.
PF04151. PPC. 1 hit.
[Graphical view]

PRINTS

PR00931. MICOLLPTASE.

SMART

SM00089. PKD. 1 hit.
[Graphical view]

SUPFAM

SSF49299. PKD. 1 hit.

PROSITE

PS50093. PKD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9X721.

Entry information

Entry name

Q9X721_CLOHI

Accession

Primary (citable) accession number: Q9X721

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1999
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)