ID A0A2A3HVF8_9ACTN Unreviewed; 764 AA.
AC A0A2A3HVF8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=microbial collagenase {ECO:0000256|ARBA:ARBA00012653};
DE EC=3.4.24.3 {ECO:0000256|ARBA:ARBA00012653};
GN ORFNames=BX265_6571 {ECO:0000313|EMBL:PBC71956.1};
OS Streptomyces sp. TLI_235.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938860 {ECO:0000313|EMBL:PBC71956.1, ECO:0000313|Proteomes:UP000218662};
RN [1] {ECO:0000313|EMBL:PBC71956.1, ECO:0000313|Proteomes:UP000218662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TLI_235 {ECO:0000313|EMBL:PBC71956.1,
RC ECO:0000313|Proteomes:UP000218662};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2017) 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:PBC71956.1}.
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DR EMBL; NSGV01000002; PBC71956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3HVF8; -.
DR Proteomes; UP000218662; 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:UP000218662};
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..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..764
FT /note="microbial collagenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012991592"
FT DOMAIN 115..296
FT /note="Peptidase M9 collagenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08453"
FT DOMAIN 681..751
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT REGION 35..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 518
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 764 AA; 82143 MW; 36691CCD72BD6D14 CRC64;
MHTSRTPSAL RALRWLALAV VCCLTLGLLL STESEAAPTA PRQTGATARS GPAPRPATTP
RPETALAPAE AAATDLADRA PQPAYDAAAT RRDKPRTAPL TSEPRSVAAP RAAACSVGDF
TGRTGAALVQ AVKAADTGCI NTLFTLTGTD ARGAFREAQM VSVADALRDV STAYPGDNST
SAAQLVLYLR AGYYVQWYHS GDVGPYGSAL QGSIRGALDA FFAAPHSRDV TDANGQSLAE
AVVLIDSAGE NARYLSVVRR LLTDYDGRYD ASWWMLSAVN NTYTVLWRGH QSPDFVAAVQ
ADHGVLDTLG AFAAGHLGML GGDRGYLVSN AGRELARFLQ HAELQGAVRP LVKDLLGRTA
MTGPTAQLWV GLAEMAAEYD AAQCAYYGTC DLANRLKAAV LTVSHTCSPS IRILAQQMTA
DQLAATCTSL AGQDAYVHGI VRDNGPVAGD RNTTIEVVVF DSSTDYRTYA GAIYGISTDN
GGMYLEGDPS AAGNQPRFIA HEAEWLRPDF QIWNLNHEYT HYLDGRFDMY GDFEAGTTTP
TIWWVEGFAE YVSYSYRGAV YTDALTQAGK HTYRLSTLFD TTYDNADTTR IYNWGYLAVR
YMTETHRADV DTLLARYRTG DWAGARALLT GTIGTRYDAD FDRWLGTCTP TGCARPECTA
TDTRRLEPGC RRSNLASPTG DYRYLYVWVP AGTARLTVTS GGGTGDADLY YSSANWATST
AYTAKAVHSG NAETLTVTNP PAGWNFVSLY AKQGFDGVWV ETAS
//
