(data stored in SCRATCH zone)

SWISSPROT: Q9FCI6_STRCO

ID   Q9FCI6_STRCO            Unreviewed;       364 AA.
AC   Q9FCI6;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   08-MAY-2019, entry version 88.
DE   RecName: Full=Endopeptidase La {ECO:0000256|PROSITE-ProRule:PRU01122};
DE            EC=3.4.21.53 {ECO:0000256|PROSITE-ProRule:PRU01122};
GN   OrderedLocusNames=SCO5202 {ECO:0000313|EMBL:CAC01332.1};
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226 {ECO:0000313|Proteomes:UP000001973};
RN   [1] {ECO:0000313|EMBL:CAC01332.1, ECO:0000313|Proteomes:UP000001973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145
RC   {ECO:0000313|Proteomes:UP000001973};
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.H., Kieser T., Larke L., Murphy L., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01122};
CC   -!- SIMILARITY: Belongs to the peptidase S16 family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01122}.
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DR   EMBL; AL939122; CAC01332.1; -; Genomic_DNA.
DR   RefSeq; NP_629350.1; NC_003888.3.
DR   RefSeq; WP_003973773.1; NC_003888.3.
DR   STRING; 100226.SCO5202; -.
DR   MEROPS; S16.012; -.
DR   EnsemblBacteria; CAC01332; CAC01332; CAC01332.
DR   GeneID; 1100643; -.
DR   KEGG; sco:SCO5202; -.
DR   PATRIC; fig|100226.15.peg.5285; -.
DR   eggNOG; ENOG4107S7F; Bacteria.
DR   eggNOG; COG3480; LUCA.
DR   HOGENOM; HOG000050560; -.
DR   InParanoid; Q9FCI6; -.
DR   KO; K07177; -.
DR   OMA; HTKMKIV; -.
DR   PhylomeDB; Q9FCI6; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10046; PTHR10046; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9FCI6.
DR   SWISS-2DPAGE; Q9FCI6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001973};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001973};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01122};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     32       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        33    364       Endopeptidase La. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004326032.
FT   DOMAIN      252    350       Lon proteolytic. {ECO:0000259|PROSITE:
FT                                PS51786}.
FT   ACT_SITE    257    257       {ECO:0000256|PROSITE-ProRule:PRU01122}.
FT   ACT_SITE    302    302       {ECO:0000256|PROSITE-ProRule:PRU01122}.
SQ   SEQUENCE   364 AA;  38181 MW;  8900C095D03C17B1 CRC64;
     MPRRTATMLA STLMLIALLC AGVFIPVPYS EMSPGPTVNT LGDHDGEPVL QISGHKTYEA
     SGHLNMTTVR VTSAEYRMNL VEAVYGWLAH DNSVVPHETL YPDGKTEEEA TQENAEEFSQ
     SQESAKVAAL KALDIPVKSW VVVSAVVKDS PSQGRLHAGD VIKAVDGTTV KKPADVAELV
     TKHEPGQDTV FTIVPAKEQA AAEKEGRTAT KTQKITIRTE TSQDAGAQRA VVGISAGTDH
     TFPFEIDIKL ADVGGPSAGL MFALGIYDKL TPGDLTGGKF VAGTGTIDDN GKVGPIGGIG
     MKTIGAHDKG AQYFLTPADN CAAAAEDTPD GLTLVKVDTI DDALGALKDI RSGKTADLPK
     CTQG
//

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