ID A0A1Q4WBI8_9ACTN Unreviewed; 772 AA.
AC A0A1Q4WBI8;
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=AMK13_12655 {ECO:0000313|EMBL:OKI07456.1};
OS Streptomyces sp. CB02056.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703924 {ECO:0000313|EMBL:OKI07456.1, ECO:0000313|Proteomes:UP000186379};
RN [1] {ECO:0000313|EMBL:OKI07456.1, ECO:0000313|Proteomes:UP000186379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02056 {ECO:0000313|EMBL:OKI07456.1,
RC ECO:0000313|Proteomes:UP000186379};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI07456.1}.
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DR EMBL; LIPD01000004; OKI07456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4WBI8; -.
DR OrthoDB; 9802683at2; -.
DR Proteomes; UP000186379; 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:UP000186379};
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..772
FT /note="microbial collagenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012840752"
FT DOMAIN 114..294
FT /note="Peptidase M9 collagenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08453"
FT DOMAIN 692..758
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT REGION 28..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 517
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 772 AA; 82969 MW; 772505C9239B85F3 CRC64;
MARLLTLVLS LFLAVGLFAP LSQAAPAGPT PGGTTPGGTP AGTPAGTAPA HLAPPPAIGE
SRADTTPAKP DGRKRLSPED LVPQSPTAPL TGLPTAGQPQ AKAFGLDAAA ARPCNVGDFT
SRTGSALVQQ IKSVDLQCVN SLFKIGRGDA ANAFRESQMV TVANAVRDAA NGYQGNDSGS
IAELMLYLQA GYFTQFYNPD VVGPYGSGLK DASRAALDAF FANPRSRDVT ADNASPLARA
ATLIDSIKDS ARYLPVVKRL LSDYDSATWN PNGMVYAVTP ALTALFAGHW EADFLPAVKA
DPSVLDALFT FISRNQGLHG GTYGRTVYEA TNELTRFMQY PDLLPRLRPY ARALAQQSAP
TGPTMYQRGS VTLAVNWWDK GNCSYYGTCD DPAKFKAANL TVKHSCSPSI VILAQALDAA
QLNTACTSLN GQDAFFHAVA KDSGPVKDDN NKTIEVVAFH SSLDYQVLAA VIYDINTNNG
GMYLEGDPAA VGNQPRFLCY EAEWARPSFE IWNLNHEYTH YLDGRFNVYG DYDAGQVQPI
DWWVEGFAEY VSYSYRKVVN DGAIAVASQH AYRLSELFDT VYATSSQDRV YRWGYLAVRY
MLEQHRSDLD AVLAKYRAGD WNGARAILKT TIGTRYDADF DSWLTKCAAG ACATDTPGQP
QLPECAGNDV RLLSADCVRG NVAATTGNYA HFYLLVPAGT KQIKVTSKGG TGNGDLYYNP
TSWAYTNAYV TRSAGPDNAE TLTVTNPPVG GYVFFSLYAQ QGFSGVSVTS EM
//