ID A0A108CJX8_9BURK Unreviewed; 644 AA.
AC A0A108CJX8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Collagenase {ECO:0000313|EMBL:KWK76133.1};
GN ORFNames=WM16_12225 {ECO:0000313|EMBL:KWK76133.1};
OS Burkholderia ubonensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=101571 {ECO:0000313|EMBL:KWK76133.1, ECO:0000313|Proteomes:UP000065504};
RN [1] {ECO:0000313|EMBL:KWK76133.1, ECO:0000313|Proteomes:UP000065504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSMB782WGS {ECO:0000313|EMBL:KWK76133.1,
RC ECO:0000313|Proteomes:UP000065504};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
RL Submitted (NOV-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:KWK76133.1}.
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DR EMBL; LPLU01000077; KWK76133.1; -; Genomic_DNA.
DR RefSeq; WP_060234535.1; NZ_LPLU01000077.1.
DR AlphaFoldDB; A0A108CJX8; -.
DR Proteomes; UP000065504; 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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..644
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007129754"
FT DOMAIN 96..247
FT /note="Peptidase M9 collagenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08453"
FT REGION 33..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 505
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 644 AA; 72066 MW; 66D9BD8AF35B478A CRC64;
MLITGMSRKT RCWSAAVALS VFTGLVGAAS ANTQPTQQKQ ARMPRVPQNL PVSPEQAEYN
LPLSEQDRAM LTRPSQQKQP LKRGKRSASG ADCRDMSVMT QYRGAALADY IANLPDYECH
YGLFSVDKTL AVQIFNAENV HAVAGRFVQE IYRYDASNLI LVNLLIYLRS AYYQYDVSGI
ADPIPNLAVQ LRPYIKQSLE GDALYRENSR APSTANELMK LITNMKDEAY YLPALKNRVA
LYTASAANPQ AAAPLQQRSA AGGFTGLLTV FFYAHQRTGA QQMLDSDATL PETLNRFVTA
NRASLSNTSA AYQLADAARE TYRFLRYPTQ KPRVKKMIQD MLASTSMTGA DSDLWLAAAE
AVDYGDSGNC TDYGTCDYKK RLADAVLTHR YACNASVRIL AQDMTAPQLQ SVCAAVARQD
DYFHRMMKTG RKPVTGDRND TIELVVFDDY ANYRKYASVI YGISTDNGGM YLEGDPSAPG
NQARFIAHEA SWLRPEFKVW NLEHEFTHYL DGRYDMAGDF TASTVKPTVW WIEGAAEYLS
RKNDNQESID AAHTGAYRFS DVLGTRYSSS DYVARAYRWG YMATRFMFER HRADVDTIVA
RFRAGDYDGY ENYVGYIGSR YDSEFADWAR NATTAGEPPL PTAR
//
