ID   A0A1H0C6J4_9ACTN        Unreviewed;       656 AA.
AC   A0A1H0C6J4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Microbial collagenase {ECO:0000313|EMBL:SDN53462.1};
GN   ORFNames=SAMN04487981_105362 {ECO:0000313|EMBL:SDN53462.1};
OS   Streptomyces sp. cf386.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1761904 {ECO:0000313|EMBL:SDN53462.1, ECO:0000313|Proteomes:UP000198720};
RN   [1] {ECO:0000313|Proteomes:UP000198720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF386 {ECO:0000313|Proteomes:UP000198720};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNHV01000005; SDN53462.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0C6J4; -.
DR   STRING; 1761904.SAMN04487981_105362; -.
DR   OrthoDB; 9802683at2; -.
DR   Proteomes; UP000198720; 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:InterPro.
DR   Gene3D; 1.10.390.20; -; 1.
DR   Gene3D; 3.40.30.160; Collagenase ColT, N-terminal domain; 1.
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   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:UP000198720};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..656
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011524027"
FT   DOMAIN          101..282
FT                   /note="Peptidase M9 collagenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08453"
FT   REGION          38..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        505
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ   SEQUENCE   656 AA;  70820 MW;  4850AB2F6A3226C3 CRC64;
     MRYRFVLPRR TLGALAVCAT LSGLLSAPAF AAPLADPDVT PTVTSPRSTT SPPPPTASLT
     DAAERTAVQK EALTPDRLPP LTPTPAQDPP PTGAVAKAKS CTPGDFGGRT GAALVAFVKA
     STTECVNTLF AVTGSDAHAV FRESQMITVA QAFTNTARTY GGDNSSRVLQ LVLFLRAGYY
     VQSNYPDDVG PYGTSLARNT TQGLDTFFAR PRSRDVTAAN GDVLGEVVVL TDSADQQARY
     LRVYQRMLNA YDSSYDAIRS MLAAVNAVHT PLWRGNWNPE YVKAVTADPS VARTLQNFAL
     AHLDLLGTDR AYLASNAGMN LARYVEHPAL RPTVRPGVRQ LLDSSRITGP TAGLWVAVAT
     QADAYDGANC TYYGVCDLTG QLMRAALPTT HDCDATHTIR AQSLTSADLA AACASVLGQD
     AYVHDLVKDD GPIPDQYLST LDLAVFTSAQ DYRTYAGAIF GISTDNGGMT VIGDPTDSAN
     KPFAVMYQKS QDTGHAARIW NLNHEYMHYL DARYNMKGDF GQQTSVPDVW WIEGVAEYVS
     YGYRRITNDQ AVAEAGRHTY RLSTLFQNTY ANSDVTRTYP WGYLAVRYMV EKHPADVQRM
     LARFRVGDYA GGYAVYATDI GTRYDADFDE WLTACAAGAC AAAPAVSRGS SRGSAR
//