ID A0A0F4K075_9ACTN Unreviewed; 795 AA.
AC A0A0F4K075;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Peptidase M9 {ECO:0000313|EMBL:KJY39504.1};
GN ORFNames=VR44_01505 {ECO:0000313|EMBL:KJY39504.1};
OS Streptomyces katrae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY39504.1, ECO:0000313|Proteomes:UP000033551};
RN [1] {ECO:0000313|EMBL:KJY39504.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY39504.1};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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}.
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:KJY39504.1}.
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DR EMBL; JZWV01000019; KJY39504.1; -; Genomic_DNA.
DR RefSeq; WP_045945494.1; NZ_JZWV01000019.1.
DR AlphaFoldDB; A0A0F4K075; -.
DR STRING; 68223.GCA_002028425_05400; -.
DR PATRIC; fig|68223.7.peg.4734; -.
DR OrthoDB; 9802683at2; -.
DR Proteomes; UP000033551; 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 Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..795
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039299633"
FT DOMAIN 151..285
FT /note="Peptidase M9 collagenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08453"
FT REGION 32..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 527
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 795 AA; 85884 MW; 5A24127265F0D0FD CRC64;
MSQHRAVRTS LLSAAVAVTL LATAGQAVTQ AAERGTPAAG PAASTPAAFA AGPAAAPNPF
DEVDRLAEAK QLDPAPAPAP GGKSVADNRV PGAADAAPAA DKGRKTATAQ AAPTAKSVAA
GVPCTLDGIT NLGPEQFADF LGDPAVTADG CLRTLIWTWD ARLAPVMSDA HVQAVSRRIS
SLAAAHDGRD SSHLEEMFTY LHAVVYHDYS RSEIDVTDAP TVDAMRRAIA DFGNAAHTFD
VTPSNARTLR EALYAGSAPG LRQHQLGLIK KVLSTLDASH PATNTDASWG GAALAALSVN
YLGVYPGNQD AAFHSAVTAD PAYRAVFKAF AGYTHLKGTA NAWAARDALG EYGRFGQVDG
LKDQITADLG ALLDPVKSSW GNGSEQWAKL VSWLNFYGAC KPYGVCKEDI EKQLFPNTYT
YDNGGIKVRT ALDRATVDQL YYASKQVKTQ FHRVLGTDQP LAGDPNSTLN IVLYASRADY
ENYHPILTGY GTNNGGIYIE NGATFYTYQR RVPQDSSLTL EELFRHEYTH YLNGRFAVPG
FFGQGDWYQG DRTTAMDEGT AEFFDGSTRD NGIAVRKSLV RGIINDTSGG GPRMSIDQLL
HATYDGDGFR FYNYAGTFFE FLWTEKPSLL REMYGYLRAN DVAGFDAWRN RMGADTYLQR
DYNRFLDAQI AKVDQLYVPN TAFTANDQLR DSALASVKSS FAAATYNTPD CVENGDTGKR
RFTCTGRITA NLKNWRSDDQ NFKDMSETVD YFILDRAGAA SNNLADMNCS FGPVEIWDNK
AAGTSSYSCE GPLRS
//
