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Database: UniProt
Entry: A0A178KM44_9GAMM
LinkDB: A0A178KM44_9GAMM
Original site: A0A178KM44_9GAMM 
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
//
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