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Database: UniProt
Entry: B5H189_STRCL
LinkDB: B5H189_STRCL
Original site: B5H189_STRCL 
ID   B5H189_STRCL            Unreviewed;       185 AA.
AC   B5H189;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=Protease {ECO:0000313|EMBL:EDY52335.1, ECO:0000313|EMBL:EFG07163.1};
GN   ORFNames=SCLAV_2090 {ECO:0000313|EMBL:EFG07163.1}, SSCG_05363
GN   {ECO:0000313|EMBL:EDY52335.1};
OS   Streptomyces clavuligerus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1901 {ECO:0000313|EMBL:EDY52335.1, ECO:0000313|Proteomes:UP000006569};
RN   [1] {ECO:0000313|EMBL:EDY52335.1, ECO:0000313|Proteomes:UP000006569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27064 {ECO:0000313|EMBL:EDY52335.1}, and ATCC 27064 / DSM
RC   738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602
RC   {ECO:0000313|Proteomes:UP000006569};
RA   Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA   Hepburn T., Sykes S., Alvarado L., Kodira C.D., Straight P., Clardy J.,
RA   Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., Lander E.,
RA   Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces clavuligerus ATCC 27064.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFG07163.1, ECO:0000313|Proteomes:UP000002357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27064 {ECO:0000313|EMBL:EFG07163.1}, and ATCC 27064 / DSM
RC   738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602
RC   {ECO:0000313|Proteomes:UP000002357};
RX   PubMed=20624727; DOI=10.1093/gbe/evq013;
RA   Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA   Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA   Breitling R., Takano E.;
RT   "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT   evolutionary reservoir of secondary metabolic pathways.";
RL   Genome Biol. Evol. 2:212-224(2010).
CC   -!- SIMILARITY: Belongs to the peptidase C56 family.
CC       {ECO:0000256|ARBA:ARBA00008542}.
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DR   EMBL; DS570694; EDY52335.1; -; Genomic_DNA.
DR   EMBL; CM000913; EFG07163.1; -; Genomic_DNA.
DR   RefSeq; WP_003958026.1; NZ_WMCC01000223.1.
DR   AlphaFoldDB; B5H189; -.
DR   STRING; 1901.BB341_17875; -.
DR   GeneID; 61471770; -.
DR   KEGG; sclf:BB341_17875; -.
DR   eggNOG; COG0693; Bacteria.
DR   OMA; YTWPADL; -.
DR   OrthoDB; 9792284at2; -.
DR   Proteomes; UP000002357; Chromosome.
DR   Proteomes; UP000006569; Unassembled WGS sequence.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03169; GATase1_PfpI_1; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR006286; C56_PfpI-like.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   NCBIfam; TIGR01382; PfpI; 1.
DR   PANTHER; PTHR42733; DJ-1 PROTEIN; 1.
DR   PANTHER; PTHR42733:SF2; DJ-1/THIJ/PFPI FAMILY PROTEIN; 1.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51276; PEPTIDASE_C56_PFPI; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EDY52335.1};
KW   Protease {ECO:0000313|EMBL:EDY52335.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002357}.
FT   DOMAIN          3..179
FT                   /note="DJ-1/PfpI"
FT                   /evidence="ECO:0000259|Pfam:PF01965"
SQ   SEQUENCE   185 AA;  20453 MW;  45234FDC65EE91E8 CRC64;
     MTAKVLIVTG DAAESLEVLY PYQRLLEEGY EVHIAAPTRK KLQFVVHDFE PGFDTYTEKP
     GYTWPADLAF SEVDPGQYTA LVIPGGRAPE YLRNDPELRK IMKAFFDADK PVAQICHGPL
     LTAAIGSLEG RRVTAYPALE LDMQAAGATF QDSEAVVDGA LVSSRAWPDH PGWMREFLKV
     LRAKG
//
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