ID A0A073KLW2_9BACI Unreviewed; 961 AA.
AC A0A073KLW2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=microbial collagenase {ECO:0000256|ARBA:ARBA00012653};
DE EC=3.4.24.3 {ECO:0000256|ARBA:ARBA00012653};
DE AltName: Full=Microbial collagenase {ECO:0000256|ARBA:ARBA00034362};
GN ORFNames=BAGA_09490 {ECO:0000313|EMBL:KEK23343.1};
OS Bacillus gaemokensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=574375 {ECO:0000313|EMBL:KEK23343.1, ECO:0000313|Proteomes:UP000027778};
RN [1] {ECO:0000313|EMBL:KEK23343.1, ECO:0000313|Proteomes:UP000027778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15801 {ECO:0000313|EMBL:KEK23343.1,
RC ECO:0000313|Proteomes:UP000027778};
RA Lai Q., Liu Y., Shao Z.;
RT "Draft genome sequence of Bacillus gaemokensis JCM 15801 (MCCC 1A00707).";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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 -!- SIMILARITY: Belongs to the peptidase M9B family. Collagenase subfamily.
CC {ECO:0000256|ARBA:ARBA00034318}.
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:KEK23343.1}.
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DR EMBL; JOTM01000017; KEK23343.1; -; Genomic_DNA.
DR RefSeq; WP_033675732.1; NZ_LTAQ01000006.1.
DR AlphaFoldDB; A0A073KLW2; -.
DR STRING; 574375.AZF08_21410; -.
DR eggNOG; COG3291; Bacteria.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000027778; 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 CDD; cd00146; PKD; 1.
DR Gene3D; 1.10.390.20; -; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.30.980.50; -; 1.
DR Gene3D; 3.40.30.160; Collagenase ColT, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR041379; ColG_subdomain.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR013661; Peptidase_M9_N_dom.
DR InterPro; IPR002169; Peptidase_M9A/M9B.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
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 Pfam; PF18911; PKD_4; 1.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00931; MICOLLPTASE.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF89260; Collagen-binding domain; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS50093; PKD; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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 Virulence {ECO:0000256|ARBA:ARBA00023026};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..961
FT /note="microbial collagenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001691362"
FT DOMAIN 769..850
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT ACT_SITE 502
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 961 AA; 110317 MW; 33FE4A9737D7EE43 CRC64;
MKKNIKFNPL ILGISTIALS LGGLQSEAFA AEKEPNNVLQ MKPIGIETSK DEIVHATKED
ETLSLEKRLK VGDFSQRPAP IMKRAETKQL QQNYSMTELN RMSNDELIDT LANIRWDQIT
DLFQFNQETK VFYQNKERMQ IIIDELGHRG STFTKEDTKG IETFVEVLRS AFYVGFYNKE
LSYLNERSFQ DKCLPALKAI AKNPNFKLGT AEQDKVVSAY GKLISNASSD AETVQYAANI
LKQYNDNFST YVSDRMKGQA VYDLMQGIDY DMQSYLYDTR KEPNATMWFG KIDNFINEVS
RIALIRNVTT ENSWLINNGI YYAGRLGKFH SNPNKGLEVI TQAMHMYPRL SEAYFGAVEQ
ITTNYGGKDS SGNTIDLEKV REEGKQQYLP KTYKFDDGSI VFKTGDKVTE EKVKRLYWAA
KEVKAQYHRV IGNDKALEQG NADDVLTIVI YNNPDEYQLN RQLYGYETNN GGIYIEEKGT
FFTYERTPEQ SIYSLEELFR HEFTHYLQGR YEVPGLFGRG DMYQNERLTW FQEGNAEFFA
GSTRTNNVVP RKSIISGLSS DPASRYTAER TLFAKYGSWD FYNYSFALQS YLYNHQFETF
DKIQDLIRAN DVKNYDVYRE TLSKDSKLNK EYQAYMQQLI DNQEKYNVPQ VSDDYLVKHA
PKALAEVKKE IVDVTNVKNA KITKHKSQFF NTFTIEGTYT GGASKGESED WKMMSKQMNQ
VLKQLSQKEW SGYKTVTAYF VNHRVNAENQ FQYDIVLHGI ATDEGENQVP NVNINGPYNG
TVNTAIQFKS DGSKGEDGKI VSYLWDFGDR KTSTEPNPIH AYEKEGTYTA TLTVKDDKGR
ENKEQTLVTV KQDTQTDIRS EEGKKISFNT IVKGKLVVPN QTDIYTFEVT SPKELNISVI
NEQQIGMTWV LHHESDMQNY VAYGQADGNV IKGQYEAKPG KYYLYVYKFD NGNGAYSLLV
K
//
