ID A0A0Q7JV58_9ACTN Unreviewed; 857 AA.
AC A0A0Q7JV58;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=microbial collagenase {ECO:0000256|ARBA:ARBA00012653};
DE EC=3.4.24.3 {ECO:0000256|ARBA:ARBA00012653};
GN ORFNames=ASD06_14780 {ECO:0000313|EMBL:KQX62164.1};
OS Angustibacter sp. Root456.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae.
OX NCBI_TaxID=1736539 {ECO:0000313|EMBL:KQX62164.1, ECO:0000313|Proteomes:UP000051170};
RN [1] {ECO:0000313|EMBL:KQX62164.1, ECO:0000313|Proteomes:UP000051170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root456 {ECO:0000313|EMBL:KQX62164.1,
RC ECO:0000313|Proteomes:UP000051170};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX62164.1, ECO:0000313|Proteomes:UP000051170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root456 {ECO:0000313|EMBL:KQX62164.1,
RC ECO:0000313|Proteomes:UP000051170};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Digestion of native collagen in the triple helical region at
CC Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for
CC Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala
CC or Arg at P3'.; EC=3.4.24.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000424};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQX62164.1}.
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DR EMBL; LMER01000020; KQX62164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q7JV58; -.
DR STRING; 1736539.ASD06_14780; -.
DR Proteomes; UP000051170; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 1.10.390.20; -; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.40.30.160; Collagenase ColT, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR013661; Peptidase_M9_N_dom.
DR InterPro; IPR002169; Peptidase_M9A/M9B.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR13062:SF9; A2M DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR13062; COLLAGENASE; 1.
DR Pfam; PF01752; Peptidase_M9; 1.
DR Pfam; PF08453; Peptidase_M9_N; 1.
DR Pfam; PF18911; PKD_4; 1.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00931; MICOLLPTASE.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS50093; PKD; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000051170};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..857
FT /note="microbial collagenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038980199"
FT DOMAIN 661..748
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 28..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 518
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 857 AA; 92032 MW; 6CF0D9C06D34F2C8 CRC64;
MGARIAAPLV CAALLTGAVG AVNAAAAPAS SGGAQRTHST KPAPAFVTGQ EDPAQEVAER
TQHPDTALTP PLSADRHRLR ARADQTRPAT ISRPSMKAQR QSAQRQSSQT AVGTCSPSDF
ASRTGSALVT QVKSSTTDCV NTLFSVSGST ARSIFNESQM VTIAYALRDV SVNYPGDAST
GAPQLVLFLR AGYYVHYYDP TTVGTYGTSL KTAIEAALDR FFASAHSQDV TDANGETLAE
AVTLIDSAEE NARYLYVVKR LLNGYNSSYD SSWWMLNAVN NTYTVLFRGH QVPAFVSAVQ
SDPSVLDTLY NFASQHLNLL GGSQSYLTSN AGRELGRFLQ HSAMQSTVRP KVAGLLNQSQ
MTGPTAPLWV GSAEMTDQYD KANCSYYNTC NLSSRLASSV LTSNYTCSSS IRILAQDMTA
SQLSSSCSSL LNQDAYFHSI VKDSGPVAND YNSTIEVVVF NSSTDYQTYA GAMYGIDTNN
GGMYLEGDPA ASGNQPRFIA YEAEWVRPTF QIWNLNHEYT HYLDGRYDMY GDFNAGVTTP
TIWWIEGFAE YVSYSYRNVT YTDALTQAGY QTYTLRQLFD TDYTADQTRI YNWGYLASRF
MITQHWADTA KVLGYYRTGQ WNAARTYLTS TIGTRYDAEF RTWLQGCAAG SCGGSTTPTP
TNQAPTASFS VSTSGLTASF TDSSSDSDGT IASRKWTFGD GSTSTATNPT KTYAAAGTYT
VQLTVTDDGG KTASTSRSVT VTSGGGTATE CTGSDDRALG QNCVRSNRSA SAGDEDYLYL
YVPAGTAKLT ITSSGGTGNA DLYYSPSSWA TPSNYTLSST NSGNSETITV NNPPSGYVYI
TLHATSSFSG VSVKTSF
//
