ID   M0QRN0_9ACTN            Unreviewed;       421 AA.
AC   M0QRN0;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000256|RuleBase:RU003567};
GN   Name=clpP {ECO:0000313|EMBL:GAC71021.1};
GN   ORFNames=GS4_47_00110 {ECO:0000313|EMBL:GAC71021.1};
OS   Gordonia soli NBRC 108243.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1223545 {ECO:0000313|EMBL:GAC71021.1, ECO:0000313|Proteomes:UP000011666};
RN   [1] {ECO:0000313|EMBL:GAC71021.1, ECO:0000313|Proteomes:UP000011666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 108243 {ECO:0000313|EMBL:GAC71021.1,
RC   ECO:0000313|Proteomes:UP000011666};
RA   Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA   Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia soli NBRC 108243.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family.
CC       {ECO:0000256|ARBA:ARBA00007039, ECO:0000256|RuleBase:RU003567}.
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:GAC71021.1}.
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DR   EMBL; BANX01000047; GAC71021.1; -; Genomic_DNA.
DR   AlphaFoldDB; M0QRN0; -.
DR   STRING; 1223545.GS4_47_00110; -.
DR   eggNOG; COG0740; Bacteria.
DR   OrthoDB; 9806592at2; -.
DR   Proteomes; UP000011666; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07016; S14_ClpP_1; 1.
DR   InterPro; IPR001907; ClpP.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR023562; ClpP/TepA.
DR   InterPro; IPR012106; Phage_Mu_Gp1.
DR   PANTHER; PTHR10381; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10381:SF70; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   Pfam; PF10123; Mu-like_Pro; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:GAC71021.1};
KW   Protease {ECO:0000313|EMBL:GAC71021.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011666}.
FT   REGION          286..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..421
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   421 AA;  44832 MW;  CDE39FAD4AD474CD CRC64;
     MNLTELLNQP AARKLDNARQ ALHPKAERRS WYEIKAPSNK ADDSTTEILI YDVIDPDPWF
     GGVSAQDFVQ GLANVDSESI LVRINSPGGD VYDALAITNA LRNHDASVTV QIDGLAASAA
     SFIAMAGDEV IVCRNSEMMI HDARGICIGS ATDMAEYAQW LHRASDNIAS IYAEKTGGEV
     KDWRKAMTAE TWYTAHEAVA AGLADRVLDD DKADSKKAAA RFDLRAYAHA GRRQAPAPFI
     PAASAGLSGK EAPVATLKEG LAERLGIDAD ADDETTLKAL EEALAERADD VTPDGGNGDT
     EPSVGDLNTA AAKHGLRLVD SAKWDEVTAQ AAAGKDARDR QVAGEQAKVV DSAISKGKIT
     SARRDHFLAL MKADTEGTTK LLADLPDETA VPLSELGHST EPDLDSVKNV REGDAYKGLE
     G
//