Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Collagenase ColA

Gene

colA

Organism
Clostridium perfringens (strain 13 / Type A)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen (By similarity).By similarity

Miscellaneous

Clostridial collagenases enable the bacteria to infiltrate and colonize host tissue, and contribute to gas gangrene (myonecrosis) pathogenesis.Curated

Catalytic activityi

Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1'; Pro and Ala at P2 and P2'; and hydroxyproline, Ala or Arg at P3'.By similarity

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds about 6 Ca2+ per subunit (Probable). The metallopeptidase and PKD domains bind 1 Ca2+, while CDB binds 2 (Probable).By similarityCurated
  • Zn2+By similarityNote: Binds 1 zinc ion.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi477Calcium 1By similarity1
Metal bindingi502Zinc; catalyticPROSITE-ProRule annotationBy similarity1
Active sitei503PROSITE-ProRule annotation1
Metal bindingi506Zinc; catalyticPROSITE-ProRule annotationBy similarity1
Metal bindingi510Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi514Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi516Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi534Zinc; catalyticBy similarity1
Metal bindingi772Calcium 2By similarity1
Metal bindingi773Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi800Calcium 2By similarity1
Metal bindingi802Calcium 2By similarity1
Metal bindingi841Calcium 2By similarity1
Metal bindingi866Calcium 3By similarity1
Metal bindingi868Calcium 3By similarity1
Metal bindingi868Calcium 4By similarity1
Metal bindingi870Calcium 4By similarity1
Metal bindingi894Calcium 3By similarity1
Metal bindingi894Calcium 4By similarity1
Metal bindingi897Calcium 3By similarity1
Metal bindingi897Calcium 4By similarity1
Metal bindingi993Calcium 5By similarity1
Metal bindingi995Calcium 5By similarity1
Metal bindingi995Calcium 6By similarity1
Metal bindingi997Calcium 6By similarity1
Metal bindingi1016Calcium 5; via carbonyl oxygenBy similarity1
Metal bindingi1020Calcium 5By similarity1
Metal bindingi1020Calcium 6By similarity1
Metal bindingi1022Calcium 6; via carbonyl oxygenBy similarity1
Metal bindingi1023Calcium 5By similarity1
Metal bindingi1023Calcium 6By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processVirulence
LigandCalcium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Collagenase ColA1 Publication (EC:3.4.24.3)
Alternative name(s):
120 kDa collagenase
Microbial collagenase
Gene namesi
Name:colA
Ordered Locus Names:CPE0173
OrganismiClostridium perfringens (strain 13 / Type A)
Taxonomic identifieri195102 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000000818 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2802

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 39Sequence analysisAdd BLAST39
PropeptideiPRO_000002867440 – 861 PublicationAdd BLAST47
ChainiPRO_000002867587 – 1104Collagenase ColAAdd BLAST1018

Keywords - PTMi

Zymogen

Interactioni

Chemistry databases

BindingDBiP43153

Structurei

3D structure databases

ProteinModelPortaliP43153
SMRiP43153
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini774 – 862PKDPROSITE-ProRule annotationAdd BLAST89

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni87 – 761S1 metalloprotease domain1 PublicationAdd BLAST675
Regioni93 – 367Activator domainBy similarityAdd BLAST275
Regioni377 – 646Catalytic subdomainBy similarityAdd BLAST270
Regioni654 – 767Helper subdomainBy similarityAdd BLAST114
Regioni762 – 860S2 domain1 PublicationAdd BLAST99
Regioni865 – 979S3a collagen-binding domain1 PublicationAdd BLAST115
Regioni992 – 1104S3b collagen-binding domain1 PublicationAdd BLAST113

Domaini

The mature protein has 4 domains; a metalloprotease domain (S1, approximately residues 87-761), S2 (762-860, equivalent to PKD), and 2 collagen-binding domains S3a (865-979) and S3b (992-1104) (PubMed:9922257). The metalloprotease S1 domain is composed of 3 subdomains which together resemble a saddle; an activator domain (residues 93-367), the catalytic peptidase subdomain (377-646) and a helper subdomain (654-767) (By similarity).By similarity1 Publication

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOGENOMiHOG000055596
KOiK01387
OMAiYEREGSY
OrthoDBiPOG091H02X9

Family and domain databases

Gene3Di2.60.40.10, 1 hit
InterProiView protein in InterPro
IPR013783 Ig-like_fold
IPR013661 Peptidase_M9_N_dom
IPR002169 Peptidase_M9A/M9B
IPR022409 PKD/Chitinase_dom
IPR000601 PKD_dom
IPR035986 PKD_dom_sf
PfamiView protein in Pfam
PF01752 Peptidase_M9, 1 hit
PF08453 Peptidase_M9_N, 1 hit
PF00801 PKD, 1 hit
PRINTSiPR00931 MICOLLPTASE
SMARTiView protein in SMART
SM00089 PKD, 1 hit
SUPFAMiSSF49299 SSF49299, 1 hit
PROSITEiView protein in PROSITE
PS50093 PKD, 1 hit
PS00142 ZINC_PROTEASE, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P43153-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKNLKRGEL TKLKLVERWS ATFTLAAFIL FNSSFKVLAA DKKVENSNNG
60 70 80 90 100
QITREINADQ ISKTELNNEV ATDNNRPLGP SIAPSRARNN KIYTFDELNR
110 120 130 140 150
MNYSDLVELI KTISYENVPD LFNFNDGSYT FFSNRDRVQA IIYGLEDSGR
160 170 180 190 200
TYTADDDKGI PTLVEFLRAG YYLGFYNKQL SYLNTPQLKN ECLPAMKAIQ
210 220 230 240 250
YNSNFRLGTK AQDGVVEALG RLIGNASADP EVINNCIYVL SDFKDNIDKY
260 270 280 290 300
GSNYSKGNAV FNLMKGIDYY TNSVIYNTKG YDAKNTEFYN RIDPYMERLE
310 320 330 340 350
SLCTIGDKLN NDNAWLVNNA LYYTGRMGKF REDPSISQRA LERAMKEYPY
360 370 380 390 400
LSYQYIEAAN DLDLNFGGKN SSGNDIDFNK IKADAREKYL PKTYTFDDGK
410 420 430 440 450
FVVKAGDKVT EEKIKRLYWA SKEVKAQFMR VVQNDKALEE GNPDDILTVV
460 470 480 490 500
IYNSPEEYKL NRIINGFSTD NGGIYIENIG TFFTYERTPE ESIYTLEELF
510 520 530 540 550
RHEFTHYLQG RYVVPGMWGQ GEFYQEGVLT WYEEGTAEFF AGSTRTDGIK
560 570 580 590 600
PRKSVTQGLA YDRNNRMSLY GVLHAKYGSW DFYNYGFALS NYMYNNNMGM
610 620 630 640 650
FNKMTNYIKN NDVSGYKDYI ASMSSDYGLN DKYQDYMDSL LNNIDNLDVP
660 670 680 690 700
LVSDEYVNGH EAKDINEITN DIKEVSNIKD LSSNVEKSQF FTTYDMRGTY
710 720 730 740 750
VGGRSQGEEN DWKDMNSKLN DILKELSKKS WNGYKTVTAY FVNHKVDGNG
760 770 780 790 800
NYVYDVVFHG MNTDTNTDVH VNKEPKAVIK SDSSVIVEEE INFDGTESKD
810 820 830 840 850
EDGEIKAYEW DFGDGEKSNE AKATHKYNKT GEYEVKLTVT DNNGGINTES
860 870 880 890 900
KKIKVVEDKP VEVINESEPN NDFEKANQIA KSNMLVKGTL SEEDYSDKYY
910 920 930 940 950
FDVAKKGNVK ITLNNLNSVG ITWTLYKEGD LNNYVLYATG NDGTVLKGEK
960 970 980 990 1000
TLEPGRYYLS VYTYDNQSGT YTVNVKGNLK NEVKETAKDA IKEVENNNDF
1010 1020 1030 1040 1050
DKAMKVDSNS KIVGTLSNDD LKDIYSIDIQ NPSDLNIVVE NLDNIKMNWL
1060 1070 1080 1090 1100
LYSADDLSNY VDYANADGNK LSNTCKLNPG KYYLCVYQFE NSGTGNYIVN

LQNK
Length:1,104
Mass (Da):125,936
Last modified:January 31, 2002 - v2
Checksum:iF4B7377194ED021C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti38L → F in BAA02941 (PubMed:8282691).Curated1
Sequence conflicti722I → M in BAA02941 (PubMed:8282691).Curated1
Sequence conflicti748G → E in BAA02941 (PubMed:8282691).Curated1
Sequence conflicti945V → E in BAA02941 (PubMed:8282691).Curated1
Sequence conflicti970T → A in BAA02941 (PubMed:8282691).Curated1
Sequence conflicti987A → E in BAA02941 (PubMed:8282691).Curated1
Sequence conflicti1098I → T in BAA02941 (PubMed:8282691).Curated1
Sequence conflicti1098I → T in BAA08848 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13791 Genomic DNA Translation: BAA02941.1
BA000016 Genomic DNA Translation: BAB79879.1
D50309 Genomic DNA Translation: BAA08848.1
PIRiA36866
RefSeqiWP_011009653.1, NC_003366.1

Genome annotation databases

EnsemblBacteriaiBAB79879; BAB79879; BAB79879
KEGGicpe:CPE0173

Similar proteinsi

Entry informationi

Entry nameiCOLA_CLOPE
AccessioniPrimary (citable) accession number: P43153
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 31, 2002
Last modified: April 25, 2018
This is version 131 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health