ID A0A5R9LQS6_9ACTN Unreviewed; 813 AA.
AC A0A5R9LQS6;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=microbial collagenase {ECO:0000256|ARBA:ARBA00012653};
DE EC=3.4.24.3 {ECO:0000256|ARBA:ARBA00012653};
GN ORFNames=C8250_040020 {ECO:0000313|EMBL:QNA78501.1};
OS Streptomyces sp. So13.3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2136173 {ECO:0000313|EMBL:QNA78501.1, ECO:0000313|Proteomes:UP000310490};
RN [1] {ECO:0000313|EMBL:QNA78501.1, ECO:0000313|Proteomes:UP000310490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So13.3 {ECO:0000313|EMBL:QNA78501.1,
RC ECO:0000313|Proteomes:UP000310490};
RX PubMed=31097761; DOI=.1038/s41598-019-43960-7;
RA Nunez-Montero K., Lamilla C., Abanto M., Maruyama F., Jorquera M.A.,
RA Santos A., Martinez-Urtaza J., Barrientos L.;
RT "Antarctic Streptomyces fildesensis So13.3 strain as a promising source for
RT antimicrobials discovery.";
RL Sci. Rep. 9:7488-7488(2019).
RN [2] {ECO:0000313|EMBL:QNA78501.1, ECO:0000313|Proteomes:UP000310490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So13.3 {ECO:0000313|EMBL:QNA78501.1,
RC ECO:0000313|Proteomes:UP000310490};
RX PubMed=32349314;
RA Nunez-Montero K., Quezada-Solis D., Khalil Z.G., Capon R.J., Andreote F.D.,
RA Barrientos L.;
RT "Genomic and Metabolomic Analysis of Antarctic Bacteria Revealed Culture
RT and Elicitation Conditions for the Production of Antimicrobial Compounds.";
RL Biomolecules 10:E673-E673(2020).
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}.
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DR EMBL; CP048835; QNA78501.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5R9LQS6; -.
DR OrthoDB; 9802683at2; -.
DR Proteomes; UP000310490; Chromosome.
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:UP000310490};
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 ACT_SITE 482
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 813 AA; 86435 MW; 2D8B60AB176DFEC3 CRC64;
MLIQPGRATA ADSRQGPATQ SPKVPPPLGS TADISDRAEV QRHPLDTAQL PPQSPVTSRA
PSKAPPRGNT ASGVAAASCT PADFSRTGSA LVAFVQASTT ACVNTLFGLT GTNAYNAFRE
AQMVTIANAF KNTARTYPGD NSGNVWQLVL FLRAGYYVQS YNSSAVGPYG PTLATASEGA
LDTFVASPHF LDVSSANGDI LGEVLVLTDS ANEQGRYLST YKRVLNAYNS SYDAYWSMDS
AVNSVFTPIF RGHWNPAYIT AVTADPSIID TLSTFALNHR DILNGSWFWL DANAGTEMAR
FLDTPALQAK VRPLAKGLLG ASSITGTTAP LWVGVAGMTD AHDQAQCSYY TTCNFTAQLT
AASLPITYPC DAGHTFRAQS LTNAALSAAC TSLKGQDAYF HGIVKDSGPV ANDNNTNIQI
VTFASPKDYQ VYSGWIFGNS TDNGGEYLEG DPATPGNQAR FLSYVKSVND GFPGDIWNLN
HEYTHYLDGR YDMYGDFTAG QGVPDIWWIE GFAEYVSYSY RNLPDTEAIA DAGQHTFALS
TLWQSTYGNS SLDRTYPWGY LAVRYMIEKH PADVQNMLAK FRTGDYNGAY AVYSTGIGTR
YDADFNTWLD ACAAGACGGT SSGPTAAFDA AVSGLTVNLT DRSTDAGSTI TARSWNFGDG
TTSTATNPAK TYTAAGTYTI TLSVTDAKGL TSTTAKPVTV SGALPTCTSA DPRVMGQNCS
RSARSASTGN LDYLYLYLPA GTTTLNITTT GGTGNADLYY NPNTWATSTA YTARSAKAGN
TEAITVTNTT AGYRYISLYA KTAFSGVTVT TKY
//
