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Protein
Submitted name:

Collagenase

Gene

colG

Organism
Clostridium histolyticum
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi795 – 7951Calcium 1Combined sources
Metal bindingi796 – 7961Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi823 – 8231Calcium 1Combined sources
Metal bindingi825 – 8251Calcium 1Combined sources
Metal bindingi864 – 8641Calcium 1Combined sources
Metal bindingi1009 – 10091Calcium 2Combined sources
Metal bindingi1011 – 10111Calcium 2Combined sources
Metal bindingi1011 – 10111Calcium 3Combined sources
Metal bindingi1013 – 10131Calcium 3Combined sources
Metal bindingi1014 – 10141Calcium 3Combined sources
Metal bindingi1032 – 10321Calcium 2; via carbonyl oxygenCombined sources
Metal bindingi1037 – 10371Calcium 2Combined sources
Metal bindingi1037 – 10371Calcium 3Combined sources
Metal bindingi1039 – 10391Calcium 3; via carbonyl oxygenCombined sources
Metal bindingi1040 – 10401Calcium 2Combined sources
Metal bindingi1040 – 10401Calcium 3Combined sources

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
  2. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources, ZincCombined sources

Enzyme and pathway databases

BRENDAi3.4.24.3. 1481.

Protein family/group databases

MEROPSiM09.002.

Names & Taxonomyi

Protein namesi
Submitted name:
CollagenaseImported
Gene namesi
Name:colGImported
OrganismiClostridium histolyticumImported
Taxonomic identifieri1498 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Subcellular locationi

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. extracellular region Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Protein family/group databases

Allergomei5989. Clo hi Collagenase.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y3UX-ray2.55A119-880[»]
2Y50X-ray2.80A119-880[»]
2Y6IX-ray3.25A119-880[»]
2Y72X-ray1.18A/B799-880[»]
3JQUX-ray1.40A/B797-881[»]
4AQOX-ray0.99A792-880[»]
4AREX-ray2.19A119-790[»]
4HPKX-ray1.35A1006-1118[»]
B1002-1118[»]
4JRWX-ray1.60A/B797-881[»]
SMRiQ9X721. Positions 1005-1118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X721.

Family & Domainsi

Keywords - Domaini

CollagenImported

Family and domain databases

Gene3Di2.60.40.670. 1 hit.
InterProiIPR007280. Peptidase_C_arc/bac.
IPR013661. Peptidase_M9_N_dom.
IPR002169. Peptidase_M9A/M9B.
IPR022409. PKD/Chitinase_dom.
IPR000601. PKD_dom.
[Graphical view]
PfamiPF01752. Peptidase_M9. 1 hit.
PF08453. Peptidase_M9_N. 1 hit.
PF00801. PKD. 1 hit.
PF04151. PPC. 1 hit.
[Graphical view]
PRINTSiPR00931. MICOLLPTASE.
SMARTiSM00089. PKD. 1 hit.
[Graphical view]
SUPFAMiSSF49299. SSF49299. 1 hit.
PROSITEiPS50093. PKD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9X721-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKNILKILM DSYSKESKIQ TVRRVTSVSL LAVYLTMNTS SLVLAKPIEN
60 70 80 90 100
TNDTSIKNVE KLRNAPNEEN SKKVEDSKND KVEHVKNIEE AKVEQVAPEV
110 120 130 140 150
KSKSTLRSAS IANTNSEKYD FEYLNGLSYT ELTNLIKNIK WNQINGLFNY
160 170 180 190 200
STGSQKFFGD KNRVQAIINA LQESGRTYTA NDMKGIETFT EVLRAGFYLG
210 220 230 240 250
YYNDGLSYLN DRNFQDKCIP AMIAIQKNPN FKLGTAVQDE VITSLGKLIG
260 270 280 290 300
NASANAEVVN NCVPVLKQFR ENLNQYAPDY VKGTAVNELI KGIEFDFSGA
310 320 330 340 350
AYEKDVKTMP WYGKIDPFIN ELKALGLYGN ITSATEWASD VGIYYLSKFG
360 370 380 390 400
LYSTNRNDIV QSLEKAVDMY KYGKIAFVAM ERITWDYDGI GSNGKKVDHD
410 420 430 440 450
KFLDDAEKHY LPKTYTFDNG TFIIRAGDKV SEEKIKRLYW ASREVKSQFH
460 470 480 490 500
RVVGNDKALE VGNADDVLTM KIFNSPEEYK FNTNINGVST DNGGLYIEPR
510 520 530 540 550
GTFYTYERTP QQSIFSLEEL FRHEYTHYLQ ARYLVDGLWG QGPFYEKNRL
560 570 580 590 600
TWFDEGTAEF FAGSTRTSGV LPRKSILGYL AKDKVDHRYS LKKTLNSGYD
610 620 630 640 650
DSDWMFYNYG FAVAHYLYEK DMPTFIKMNK AILNTDVKSY DEIIKKLSDD
660 670 680 690 700
ANKNTEYQNH IQELADKYQG AGIPLVSDDY LKDHGYKKAS EVYSEISKAA
710 720 730 740 750
SLTNTSVTAE KSQYFNTFTL RGTYTGETSK GEFKDWDEMS KKLDGTLESL
760 770 780 790 800
AKNSWSGYKT LTAYFTNYRV TSDNKVQYDV VFHGVLTDNA DISNNKAPIA
810 820 830 840 850
KVTGPSTGAV GRNIEFSGKD SKDEDGKIVS YDWDFGDGAT SRGKNSVHAY
860 870 880 890 900
KKAGTYNVTL KVTDDKGATA TESFTIEIKN EDTTTPITKE MEPNDDIKEA
910 920 930 940 950
NGPIVEGVTV KGDLNGSDDA DTFYFDVKED GDVTIELPYS GSSNFTWLVY
960 970 980 990 1000
KEGDDQNHIA SGIDKNNSKV GTFKSTKGRH YVFIYKHDSA SNISYSLNIK
1010 1020 1030 1040 1050
GLGNEKLKEK ENNDSSDKAT VIPNFNTTMQ GSLLGDDSRD YYSFEVKEEG
1060 1070 1080 1090 1100
EVNIELDKKD EFGVTWTLHP ESNINDRITY GQVDGNKVSN KVKLRPGKYY
1110
LLVYKYSGSG NYELRVNK
Length:1,118
Mass (Da):126,242
Last modified:October 31, 1999 - v1
Checksum:i770CF3F60E4D4FD4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87215 Genomic DNA. Translation: BAA77453.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87215 Genomic DNA. Translation: BAA77453.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y3UX-ray2.55A119-880[»]
2Y50X-ray2.80A119-880[»]
2Y6IX-ray3.25A119-880[»]
2Y72X-ray1.18A/B799-880[»]
3JQUX-ray1.40A/B797-881[»]
4AQOX-ray0.99A792-880[»]
4AREX-ray2.19A119-790[»]
4HPKX-ray1.35A1006-1118[»]
B1002-1118[»]
4JRWX-ray1.60A/B797-881[»]
SMRiQ9X721. Positions 1005-1118.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL2268009.

Protein family/group databases

Allergomei5989. Clo hi Collagenase.
MEROPSiM09.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.24.3. 1481.

Miscellaneous databases

EvolutionaryTraceiQ9X721.

Family and domain databases

Gene3Di2.60.40.670. 1 hit.
InterProiIPR007280. Peptidase_C_arc/bac.
IPR013661. Peptidase_M9_N_dom.
IPR002169. Peptidase_M9A/M9B.
IPR022409. PKD/Chitinase_dom.
IPR000601. PKD_dom.
[Graphical view]
PfamiPF01752. Peptidase_M9. 1 hit.
PF08453. Peptidase_M9_N. 1 hit.
PF00801. PKD. 1 hit.
PF04151. PPC. 1 hit.
[Graphical view]
PRINTSiPR00931. MICOLLPTASE.
SMARTiSM00089. PKD. 1 hit.
[Graphical view]
SUPFAMiSSF49299. SSF49299. 1 hit.
PROSITEiPS50093. PKD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: JCM 1403Imported.
  2. "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 (AUG-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 797-881.
  3. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) OF 799-880 IN COMPLEX WITH ZINC.
  4. "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(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1006-1118 AND 1002-1118 IN COMPLEX WITH CALCIUM.
  5. "Structural basis for activity regulation and substrate preference of clostridial collagenases G, H, and T."
    Eckhard U., Schonauer E., Brandstetter H.
    J. Biol. Chem. 288:20184-20194(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (0.99 ANGSTROMS) OF 792-880 IN COMPLEX WITH CALCIUM AND ZINC.
  6. "Crystal structure of Clostridium histolyticum colg collagenase PKD domain 2 at 1.6 Angstrom resolution."
    Sakon J., Philominathan S.T.L., Gann S., Bauer R., Matsushita O.
    Submitted (FEB-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 797-881.

Entry informationi

Entry nameiQ9X721_CLOHI
AccessioniPrimary (citable) accession number: Q9X721
Entry historyi
Integrated into UniProtKB/TrEMBL: October 31, 1999
Last sequence update: October 31, 1999
Last modified: March 31, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.