ID A0A178K8X5_9GAMM Unreviewed; 810 AA.
AC A0A178K8X5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=microbial collagenase {ECO:0000256|ARBA:ARBA00012653};
DE EC=3.4.24.3 {ECO:0000256|ARBA:ARBA00012653};
GN ORFNames=A3K86_14730 {ECO:0000313|EMBL:OAN13810.1};
OS Photobacterium jeanii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=858640 {ECO:0000313|EMBL:OAN13810.1, ECO:0000313|Proteomes:UP000078503};
RN [1] {ECO:0000313|EMBL:OAN13810.1, ECO:0000313|Proteomes:UP000078503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-40508 {ECO:0000313|EMBL:OAN13810.1,
RC ECO:0000313|Proteomes:UP000078503};
RA Li Y.;
RT "Photobacterium proteolyticum sp. nov. a protease producing bacterium
RT isolated from ocean sediments of Laizhou Bay.";
RL Submitted (MAR-2016) 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=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:OAN13810.1}.
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DR EMBL; LVHF01000028; OAN13810.1; -; Genomic_DNA.
DR RefSeq; WP_068332522.1; NZ_PYMD01000001.1.
DR AlphaFoldDB; A0A178K8X5; -.
DR STRING; 858640.A3K86_14730; -.
DR OrthoDB; 9802683at2; -.
DR Proteomes; UP000078503; 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 Gene3D; 1.10.390.20; -; 1.
DR Gene3D; 2.60.120.380; -; 2.
DR Gene3D; 3.40.30.160; Collagenase ColT, N-terminal domain; 1.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
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 Pfam; PF04151; PPC; 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:UP000078503};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..810
FT /note="microbial collagenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008090097"
FT DOMAIN 40..212
FT /note="Peptidase M9 collagenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08453"
FT DOMAIN 597..669
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT ACT_SITE 436
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 810 AA; 91455 MW; 7CC2D98A382A3A1D CRC64;
MTYSNTFKRS ALALVLSSFC YTSSVFAAPT CEVNALLTTQ NPLNAVESAD LDCRNNWFST
TATQAQTIFS DQLVEQAQVR LQAAVNSYSG EKEQAIIINN FGEYIRAAYY VRSNNQAQLG
NFSDELDIKL AQTINSFITS PHAINYGYEQ SAALKSMTIM VDNIRRLPLT MANQLALLQH
FTPESIEHSR FIEALNDLFR GMSGHTGNDA FYADLAKHPE YLRQLEQFIY DNEWALDTSA
SFIVSNASRE MGRLLASPYP ETKQAILAIQ NNLLKRYPLG GKSDKIWVGI AEMVHYFAPD
QAEAMGLKDG KAKLETMVMP FTYRCDGPAI VRAQKMDQAQ AAEVCTTLNA KEADFHQVVN
SNSIPVADDN NDKVEVIVFD TNSDYVTYSN FLFGNTTDNG GQYLEGNPAD PNNTARFVAY
RNEYAEGFSI LNLEHEYVHY LDGRFNLYGD FGDVLREGST VWWLEGFAEY MHYKEGYNAA
IELGKTHQYT LPEVIATTYS HDTNRVYRWG YLAVRFFIEN HPQEIEQLLS LSRNNQFKAW
AKKSQELGQQ YQQEFDTWID TLKVSKEPNK PGNNEPTAKA LALNTGTVLE GERHSAHHFY
IDVPEYTRSL ELSIQGEGDA DLYASFDRMA YYHDYDFSSF TYGSNEQVTI EPQENGYVKA
GRYYISVDGR EAFNAVELMA KAEVENKGNN GGNQGGNTQQ DDLAPIVLNA DEPVKLDIIN
TRYMALYVPE GKETVRIWVT PTAQTAKLES NVDLFASQAH WPTPEQHDAA SQYTGSREFI
EMQVEQAGYV HFMMSNNGQK EEVEIYATAY
//
