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Database: UniProt
Entry: A0A512B1L0_9BACT
LinkDB: A0A512B1L0_9BACT
Original site: A0A512B1L0_9BACT 
ID   A0A512B1L0_9BACT        Unreviewed;       857 AA.
AC   A0A512B1L0;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   03-MAY-2023, entry version 13.
DE   SubName: Full=ATP-dependent Clp protease ClpC {ECO:0000313|EMBL:GEO05868.1};
GN   Name=clpC {ECO:0000313|EMBL:GEO05868.1};
GN   ORFNames=AAE02nite_35320 {ECO:0000313|EMBL:GEO05868.1};
OS   Adhaeribacter aerolatus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Adhaeribacter.
OX   NCBI_TaxID=670289 {ECO:0000313|EMBL:GEO05868.1, ECO:0000313|Proteomes:UP000321532};
RN   [1] {ECO:0000313|EMBL:GEO05868.1, ECO:0000313|Proteomes:UP000321532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 106133 {ECO:0000313|EMBL:GEO05868.1,
RC   ECO:0000313|Proteomes:UP000321532};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Adhaeribacter aerolatus NBRC 106133.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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:GEO05868.1}.
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DR   EMBL; BJYS01000028; GEO05868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A512B1L0; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000321532; 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: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:SF18; HEAT SHOCK PROTEIN 104; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:GEO05868.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:GEO05868.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000321532};
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          441..476
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          143..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          829..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          437..487
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        829..847
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   857 AA;  95924 MW;  C8612C37A604F244 CRC64;
     MEAKFSNRVK EVISLSREEA IRLGHDYIGT EHLLLGMIRE GEGTAITLLK KLGVSIDELK
     YALEQATRNT ASHNTSITGS IPLTKQTEKV LKITYLEAKI FKSDIIGTEH LLLSILRDED
     NISSQTLAKF NVNYEAIRDS LDYQNNNPMA SSDTDDDNDN DKLFGSSGSA KGSTAKKPGE
     KSRTPVLDNF GRDLTKLAED DKLDPIVGRE KEIERVAQVL SRRKKNNPIL IGEPGVGKTA
     IAEGLALRIV QKKVSRVLFN KRVVTLDLAS LVAGTKYRGQ FEERMKAVMN ELEKSPDVIL
     FIDELHTIVG AGGASGSLDA SNMFKPALAR GEIQCIGATT LDEYRQYIEK DGALARRFQI
     VMVDPTTPEE TIEILNNIKD KYQDHHHVIY TDKAIEACVK LSDRYMSDRF LPDKAIDILD
     EAGARVHINN IVVPEDILKL EEQIENIKTE KNRVVKSQKY EEAAQLRDKE KRLLDQLDIA
     KKNWEDETKK KRYTVKEENV AEVIAMMTGI PVKRIAQNES QKLLSMGDEL QDKVIGQEKA
     IKQLVKAIQR TRVGLKDPKK PIGSFVFLGP TGVGKTELAK VLATYLFDKE DALVRIDMSE
     YMEKFSVSRL VGAPPGYVGY EEGGQLTEKI RRKPYSVILL DEIEKAHPDI YNLLLQVLDD
     GVLTDGLGRK VDFRNTIIIM TSNIGARDLQ DFGAGIGFST KAKQENLDDI MRGTISNALK
     KTFSPEFLNR LDDVIVFNSL GREDIHKIID ISLSKLFKRL ETLGYKIELT DKAKDFVAEK
     GYDPKYGARP LNRAIQKYLE DPIAEEILRA DVSNGDIIIA DFEEGKETLT FRSESSGKPK
     LPEESSESTP ADPKTGE
//
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