ID   A0A0X8JC53_9FLAO        Unreviewed;       847 AA.
AC   A0A0X8JC53;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:AMD85738.1};
GN   ORFNames=AXF12_09570 {ECO:0000313|EMBL:AMD85738.1};
OS   Capnocytophaga haemolytica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=45243 {ECO:0000313|EMBL:AMD85738.1, ECO:0000313|Proteomes:UP000065822};
RN   [1] {ECO:0000313|Proteomes:UP000065822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 32990 {ECO:0000313|Proteomes:UP000065822};
RA   Holder M.E., Ajami N.J., Petrosino J.F.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP014227; AMD85738.1; -; Genomic_DNA.
DR   RefSeq; WP_066430617.1; NZ_LT906449.1.
DR   AlphaFoldDB; A0A0X8JC53; -.
DR   STRING; 45243.AXF12_09570; -.
DR   KEGG; chg:AXF12_09570; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000065822; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001943; UVR_dom.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF193; CHAPERONE PROTEIN CLPB; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Hydrolase {ECO:0000313|EMBL:AMD85738.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AMD85738.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          451..486
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          169..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   847 AA;  96005 MW;  257DED2889DD79F6 CRC64;
     MNDNFSPRVK RIFTYSKDEA IRLGQSTVGT EHFILAMLQE GEGRAIEILQ NLGVDIEKLR
     QQIHTLTSVR GLSPANYNSI HFTIQAERAM QTTYLEAKRT QNDVINTAHL LLSILRNEND
     PTTKIFNKIG VNYDLVRNNL QSSQHEGGYL VNSVEEFDSY ERDYRLPQND RINRVNNDKD
     AQENDANGQR QRKLTVLDNF GRDLTTLAEQ GKLDPVVGRE KEIERVSQIL SRRKKNNPLL
     IGEPGVGKSA IAEGLALRIY EKKVSRVLFN KRVVTLDLAS LVAGTKYRGQ FEERMKAIMN
     ELEKNNDIIL FIDEIHTLVG AGGASGTLDA SNMFKPALAR GEVQCIGATT LDEYRQSIEK
     DGALERRFQK VIVEPTSVEE TIQILRNVKR QYEEHHNVTY TEGAIEACVK LTNRYITDRY
     LPDKALDALD EAGARIHINH LKIPKHITDM EERLSQAVKA KSNAVQHQQF EEAARLRDNE
     RGLEQALAEM NQKWQEESKL HRDVVTEEHI ADVVSMMSGV PVNRIAQTEM NKLGTLAQTM
     KAKIIGQDEA VDKVVKAIKR NRTGLKDPNK PIGSFIFLGQ TGVGKTQLAK VLARELFDSE
     ETMVRIDMSE YMEKFSVSRL IGAPPGYVGY EEGGQLTEKI RRKPYSVVLL DEIEKAHPDV
     FNMLLQVLDD GFLTDSLGRK IDFRNTIIIM TSNIGARQVK DFGQGVGFGT SARASQSEAN
     EKSIIENALK KVFAPEFLNR VDDVVMFNPL SKEDIFRIID IELGKLYSRI QDLGYAIKLS
     DKAKEFIAEK GYDKQYGARP LKRAIQKYVE DLLAEEIVTS QIKQGDYVHF DMDEANEHLM
     IKERTFI
//