ID   A0A1B8UM14_9BACL        Unreviewed;      1040 AA.
AC   A0A1B8UM14;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Peptidase M9 {ECO:0000313|EMBL:OBY77401.1};
GN   ORFNames=BBG47_22010 {ECO:0000313|EMBL:OBY77401.1};
OS   Paenibacillus sp. KS1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1849249 {ECO:0000313|EMBL:OBY77401.1, ECO:0000313|Proteomes:UP000092663};
RN   [1] {ECO:0000313|EMBL:OBY77401.1, ECO:0000313|Proteomes:UP000092663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KS1 {ECO:0000313|EMBL:OBY77401.1,
RC   ECO:0000313|Proteomes:UP000092663};
RA   Lata P., Govindarajan S., Qi F., Li J.-L., Sahoo M.K.;
RT   "Deep sequencing identified Paenibacillus in Kanamycin resistant culture
RT   isolate from epiphyte Tillandsia usneoides (Spanish moss) in central
RT   Florida, USA.";
RL   Submitted (JUN-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}.
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:OBY77401.1}.
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DR   EMBL; MAIS01000082; OBY77401.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8UM14; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000092663; 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; 2.60.120.380; -; 2.
DR   Gene3D; 3.30.980.50; -; 1.
DR   Gene3D; 3.40.30.160; Collagenase ColT, N-terminal domain; 1.
DR   InterPro; IPR041379; ColG_subdomain.
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; PF18496; ColG_sub; 1.
DR   Pfam; PF01752; Peptidase_M9; 1.
DR   Pfam; PF08453; Peptidase_M9_N; 1.
DR   PRINTS; PR00931; MICOLLPTASE.
DR   SUPFAM; SSF89260; Collagen-binding domain; 2.
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:UP000092663};
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..1040
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038750919"
FT   DOMAIN          99..274
FT                   /note="Peptidase M9 collagenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08453"
FT   DOMAIN          652..766
FT                   /note="Collagenase ColG-like catalytic helper subdomain"
FT                   /evidence="ECO:0000259|Pfam:PF18496"
FT   REGION          55..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          767..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        780..796
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        504
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ   SEQUENCE   1040 AA;  117850 MW;  38469C93B2D55416 CRC64;
     MKEQRKQRAW MKWTSILLAA TVATGSTAGF AAAEERGLQV REDAAQFGIH NVIAQQEPSG
     SDLPSDMEGR LPMAEQSEDP GIPEPPARAV KSISEQSTYS MADLNALSYE ELTDLLVSID
     WEKIPELFKL NEDSRRFYAD ENRMQAIIDR LEESGRRFTT EDMKGIPTLV EVLRSGVYLG
     YYNKELSRLN ELDFREKMLP AIKAIIDNPS FTWGNEVQHS VISATGRLIS NVTVDTYIVN
     RLTGLLSDFT DRQEQLGGNF LSGKAFYDVI QGVGYVLMYR MTEPDQKAEF KGNIDGYLEQ
     LFRLGSEGST AEDKKWLTSN AIYYSGALGH YHSDPEKANR VLTDVMQTQP KLGEFYFVAA
     DQIARNYDEK DAYGNRVDID ELKQRGKEHY LPQRVEFDDG QIVFRAGGQL TQEQLQRLYW
     AAKEVKAQFH RVIGNDKPLE AGNADDVLTI VIYNSPDEYK MNKFLYGYDT ENGGIYIEGV
     GTFFTYDRTE NQSIYSLEEL FRHEFTHYLQ ARFEVPGQFG QGPLYQGGRM QWFDEGGAEF
     FAGATRMEGI KPRKSVVGYL VGDEPGQRFT VSDTVNSKYG SWQFYNYSFA LYDYLYHHDF
     NAMDRIHRAI RYNDANAYEQ QLASISGDAR TNESYQRSID EAVARYEELS TPLVSDDYLQ
     AVEQKPELEI YDEITNVAEL RNRSVKKSNS GLFQTFELRG TYVGGASAGI EQDWQTMNKL
     TDGFLHTLSD KPWNGFKTVT AYFTNYRVND EGNFVYDVVF NGKLPEGTDS GKDVVLPDGG
     TNSGNGNNSN SGNKDGDRQP DVTDREPNDT WKTAIRLDGT GKSVSGKVSD TDALDVYRFD
     AKQAGEWMIE LESAQERGVA WVLFHESDQD NYKAYPTKIE GNSLAGSISV DEPGTYYLHV
     YAIAEGDQTY NLVVKPEGQQ QPESELSLFE ETEPNDALDM ANGPVPFGRT IMGTLESDDQ
     QDIFVIDVDK PRALNIALEK QLGDHVNWVL YRESDNEQIL YPVDEDGNFM KGEVEAEPGR
     YHLYVYKFAD EDVHYKLQIK
//