ID A0A1R1SFK0_9ACTN Unreviewed; 693 AA.
AC A0A1R1SFK0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=microbial collagenase {ECO:0000256|ARBA:ARBA00012653};
DE EC=3.4.24.3 {ECO:0000256|ARBA:ARBA00012653};
GN ORFNames=SPAR_23546 {ECO:0000313|EMBL:OMI36968.1};
OS Streptomyces sparsogenes DSM 40356.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1331668 {ECO:0000313|EMBL:OMI36968.1, ECO:0000313|Proteomes:UP000186168};
RN [1] {ECO:0000313|EMBL:OMI36968.1, ECO:0000313|Proteomes:UP000186168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40356 {ECO:0000313|EMBL:OMI36968.1,
RC ECO:0000313|Proteomes:UP000186168};
RA Coyne S., Seebeck F.P.;
RT "Genome sequence of Streptomyces sparsogenes DSM 40356.";
RL Submitted (MAY-2013) 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:OMI36968.1}.
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DR EMBL; ASQP01000320; OMI36968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1SFK0; -.
DR STRING; 67365.GCA_001704635_04271; -.
DR Proteomes; UP000186168; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR013661; Peptidase_M9_N_dom.
DR InterPro; IPR002169; Peptidase_M9A/M9B.
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; PF04151; PPC; 1.
DR PRINTS; PR00931; MICOLLPTASE.
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:UP000186168};
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 42..225
FT /note="Peptidase M9 collagenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08453"
FT DOMAIN 610..680
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 446
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 693 AA; 75408 MW; E98F5B6446C56E8F CRC64;
MPAKLRGGPA ALGSAKPSKP HLSTHATLDA AGATQPAAVT SCTTSDFSSR SGSDLVSYIK
TVDWRSCINP LFSLTGSDAH AVFKQSQMLA VSNGIARAAG SYTGDDSGGL YELMYFMRAG
YYVQYGDPQD VGPYDSSLRS AIENGFNTLF ASSHANDISA GNGAVLEQAF ILTDSAQVQA
DYLDVYGRYL NAYTSSSWDA VPEMDRALNA IYTPLWRGPW LSDFVTAIIA DSSIADTLYK
FTLNHRDLLG GNNDVLDSNA GNDLANFIQI PALRSKIRPL VKGLLDGSSM TGATNNLWVH
VAYRAGTGDP DHCSYYGVCD LRKQLTAAAL PINYACSNFT IMAQALTAKE QSDVCTSLSN
EVAFYQNQVK TTTPIPGEYF NLKMVIFGSR ADYVTYSWAI FGNDTNNGGE TLTGTPTDPN
NIAYSILYQW PTDNGFTARA WNLNHEFAHV QQSIYDMKGD FGTQITVPDV WWIEGQAEYV
SYTYRNLTDN GALTEAARHT YKLSQLFQNT YTIDDETRTY PWGYLAVRYM TEKHPDRIQA
MLAKMRTGDY QGAYAVYNNI GTSYDADFDA WLDTLGGGNG GGSTTACTGT NPQAMGQNCF
RSNQSRVAGD TDYLWIWLPA GTTTLKVTTS GGSGNADLYY DPTTWAGPST FTEKSTNPGN
TESITVSNTE AGYRYISLYA VTDFSGVTVS TSF
//
