ID A0A561EXY0_9ACTN Unreviewed; 833 AA.
AC A0A561EXY0;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=microbial collagenase {ECO:0000256|ARBA:ARBA00012653};
DE EC=3.4.24.3 {ECO:0000256|ARBA:ARBA00012653};
GN ORFNames=FB465_5613 {ECO:0000313|EMBL:TWE20459.1};
OS Kitasatospora atroaurantiaca.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=285545 {ECO:0000313|EMBL:TWE20459.1, ECO:0000313|Proteomes:UP000318416};
RN [1] {ECO:0000313|EMBL:TWE20459.1, ECO:0000313|Proteomes:UP000318416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41649 {ECO:0000313|EMBL:TWE20459.1,
RC ECO:0000313|Proteomes:UP000318416};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JUN-2019) 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:TWE20459.1}.
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DR EMBL; VIVR01000001; TWE20459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A561EXY0; -.
DR OrthoDB; 9802683at2; -.
DR Proteomes; UP000318416; 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:UP000318416};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 641..721
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 36..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 501
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 833 AA; 88914 MW; D52AB251E091235A CRC64;
MRTAPARKDL VRLLIAALVC CLGITLLAPA GHARASAPAA GRTTPSVPPP QPASADSASQ
KMDSEDKPVD AAHRPPLRPV AEAREHGAAS PHLTAAACNV ADFTGRTGDA LVQQIKASST
DCVNTLFGLT GNDAYAAFRE AQMTSVAYGL RDVSATYPGD NSTSAAQLVL FLRAGYFVHW
YNASTVGTYG PALQTAIRAG LDAFFGNAHS RDVTDANGQS LAEAVTLIDS AEENARYLDV
VKRLLAGYTT AYNSSYWMLA AVNNVYTVLW RGHQSPDFVA AVQADPSVTD ALYDFATANN
ALLGTGQAYL TANAGRELGR FLQHTALQGK VRPLVKDLLG QSAITGRTAP LWVGLAEMTD
SFDKANCAYY DTCDLPARLR SAVLTTTFTC SPSIRIVAQQ MTPAELDSTC TSLRNQDAYV
HGIVKDKGPV ANDNNATIEV VVFDSSADYQ TYAGEIFGIS TNNGGMYLEG DPAAAGNQPR
FVAYEAEWLR PAFQIWNLNH EYTHYLDGRF DMYGDFDAGV STPTIWWIEG FAEYVSYSYR
NVSYDAAIAQ AAKGTYKLST LFDTTYDNDT TRIYNWGYLA VRYMLQSHRA DVDTLLGYYR
TGDWSAARTL LTSTIGTRYD ADWSAWLAAC AAGNCGSVTP VNQPPSAGFA AVVSGLKVSF
TDRSTDADGT IVSRKWSFGD GTGSTAANPS KTYAKAGTYT VKLTVTDDKG ATATAAQAVT
VAGLPECSAA DNRELGKKCR RSNLAATTGN YSYLYLVVPA GTSRLKITSA GGTGNADLYY
SAKGWATTTS YTQRSVKAGN AETLTVTNPP AGTVFISLYA KQGFASVAVT TEF
//
