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Database: UniProt
Entry: C3JBC6_POREA
LinkDB: C3JBC6_POREA
Original site: C3JBC6_POREA 
ID   C3JBC6_POREA            Unreviewed;       420 AA.
AC   C3JBC6;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=ATP-dependent Clp protease, ATP-binding subunit ClpX {ECO:0000313|EMBL:EEN82407.1};
GN   Name=clpX {ECO:0000313|EMBL:EEN82407.1};
GN   ORFNames=POREN0001_1659 {ECO:0000313|EMBL:EEN82407.1};
OS   Porphyromonas endodontalis (strain ATCC 35406 / BCRC 14492 / JCM 8526 /
OS   NCTC 13058 / HG 370).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=553175 {ECO:0000313|EMBL:EEN82407.1, ECO:0000313|Proteomes:UP000004295};
RN   [1] {ECO:0000313|EMBL:EEN82407.1, ECO:0000313|Proteomes:UP000004295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35406 / BCRC 14492 / JCM 8526 / NCTC 13058 / HG 370
RC   {ECO:0000313|Proteomes:UP000004295};
RA   Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01250}.
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:EEN82407.1}.
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DR   EMBL; ACNN01000026; EEN82407.1; -; Genomic_DNA.
DR   RefSeq; WP_004334219.1; NZ_ACNN01000026.1.
DR   AlphaFoldDB; C3JBC6; -.
DR   STRING; 553175.POREN0001_1659; -.
DR   GeneID; 84818220; -.
DR   eggNOG; COG1219; Bacteria.
DR   Proteomes; UP000004295; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19497; RecA-like_ClpX; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 6.20.220.10; ClpX chaperone, C4-type zinc finger domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   InterPro; IPR038366; Znf_CppX_C4_sf.
DR   NCBIfam; TIGR00382; clpX; 1.
DR   PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   Pfam; PF06689; zf-C4_ClpX; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SMART; SM00994; zf-C4_ClpX; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51902; CLPX_ZB; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:EEN82407.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PROSITE-
KW   ProRule:PRU01250}; Hydrolase {ECO:0000313|EMBL:EEN82407.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01250}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:EEN82407.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004295};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01250}.
FT   DOMAIN          1..55
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01250"
SQ   SEQUENCE   420 AA;  47033 MW;  41FCBAC75FE80BE6 CRC64;
     MAPKKKDGNH KHCSYCGRGE EDVNFLIQGE EGVAICDLCI NEMNKMIRQA MGPTPVDSTV
     ENPPKADLCF EKLPRPKDIK AFLDQYVVGQ DAAKKYLSVA VYNHYKRVLQ VPNDEDIEVE
     KSNIIMVGPT GTGKTLLAQT IARMLDVPFA IADATVLTEA GYVGEDIESI LTRLLQSCNY
     DERAAERGIV FIDEIDKIAR KSDNPSITRD VSGEGVQQGL LKLLEGSIIN VPPAGGRKHP
     DQKFIHVNTR HILFICAGAF DGIERKIANR LNTRYIGYQE EGERSHVDPQ HLLKHVSHQD
     LRAYGLIPEI LGRLPILTYL DPLERSTLKS ILTEPKNAII GQYVKLFAMD GIKLHFTDEA
     LDYIVDKTIK EELGARGLRS VVETIMMEAM YTLPGNTDVS ELLVTREYAQ EHSKELHIRN
//
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