ID A0A178KM44_9GAMM Unreviewed; 817 AA.
AC A0A178KM44;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, 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};
GN ORFNames=A3K86_01540 {ECO:0000313|EMBL:OAN17632.1};
OS Photobacterium jeanii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=858640 {ECO:0000313|EMBL:OAN17632.1, ECO:0000313|Proteomes:UP000078503};
RN [1] {ECO:0000313|EMBL:OAN17632.1, ECO:0000313|Proteomes:UP000078503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-40508 {ECO:0000313|EMBL:OAN17632.1,
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:OAN17632.1}.
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DR EMBL; LVHF01000012; OAN17632.1; -; Genomic_DNA.
DR RefSeq; WP_068326654.1; NZ_PYMD01000001.1.
DR AlphaFoldDB; A0A178KM44; -.
DR STRING; 858640.A3K86_01540; -.
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 CDD; cd00146; PKD; 1.
DR Gene3D; 1.10.390.20; -; 1.
DR Gene3D; 3.40.30.160; Collagenase ColT, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; 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; SSF49299; PKD domain; 1.
DR PROSITE; PS50093; PKD; 1.
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..817
FT /note="microbial collagenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008090497"
FT DOMAIN 614..702
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT ACT_SITE 481
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 817 AA; 91903 MW; 86733B6F6009DDBD CRC64;
MKIYKLNLVL VGLLLSLNVN AYSEPTSQMV ENQDLQYHHT HGVESQLIER SPVAVLPQQT
KEESDKFVSM NRVSAFDAVE TCDLNAFVNA SNISDAIKEQ GTDCINKLFS ASSDIQVAAF
DSGNMYNAAK HTAQLARAYN GGGSKDLQAL YLYLRAGYYA EYYNKNIDFL PWVTPAVKEA
LDAFVNNANF YENSDQHGKV LSEMITTIDS ANLQHEYIHV LTQWLTRWNQ NYAKNWSMRN
AVNGIFTVLY RGQWNKAFVS AIGSETNLVN ALAEFALNQS AVGADDEFMA ANAGRELGRF
TMYKNTAIQP LVKSKLKEIF NRYNMYGYGD AIWLATADTT SHHSDCSEYG ICDFEPKLKK
LVLSQSYTCS DSLRILSQDM TSEQHQSACD KLGYEESYFH TLLETGNQPV EDDVNTQLQV
NIFNSSNDYQ KYAGVIFGIN TDNGGMYLEG DPSKPGNVPN FVAYEAAKAN PDHYVWNLEH
EYVHYLDGRF NMYGNFGSPT EKVVWWSEGI AEYVANEDDN PRAIDTIKDG SVYTLNEIFE
TTYDGFDVDR IYRWGYLAVR FMFNRHKDEI NRMLIETRQG DWSGYKAIIN GWQNLYQAEF
EEWQQELISN KSGKPVAVID AVNKAKVDTD ISFSSANSSD KDGVITQYLW NFGDGTTSDA
ANPTHKYASV GNYVVTLTVT DDSGLTGSAK LPISVVNEVS NDRFPINCSA ENKVTSGRLE
VGKYVCLGSD QTIWLSIPEV NKHQTMSITT ANGTGDMKLE YSNFDWPNGS NLHAWSDRAG
NDECITLNWQ DQYWGYLKIS GEFENAAIIV DFDKGCR
//