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Database: UniProt
Entry: A0A1T5J5M5_9BACT
LinkDB: A0A1T5J5M5_9BACT
Original site: A0A1T5J5M5_9BACT 
ID   A0A1T5J5M5_9BACT        Unreviewed;       781 AA.
AC   A0A1T5J5M5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SKC46705.1};
GN   ORFNames=SAMN06298215_1061 {ECO:0000313|EMBL:SKC46705.1};
OS   Bacteroidales bacterium WCE2008.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1945891 {ECO:0000313|EMBL:SKC46705.1, ECO:0000313|Proteomes:UP000190446};
RN   [1] {ECO:0000313|EMBL:SKC46705.1, ECO:0000313|Proteomes:UP000190446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCE2008 {ECO:0000313|EMBL:SKC46705.1,
RC   ECO:0000313|Proteomes:UP000190446};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUZM01000003; SKC46705.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5J5M5; -.
DR   STRING; 1945891.SAMN06298215_1061; -.
DR   Proteomes; UP000190446; 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   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   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; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 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:SKC46705.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SKC46705.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190446};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          221..366
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          497..675
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          674..772
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          147..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   781 AA;  86533 MW;  196188F33FD10B53 CRC64;
     MDITVSEELN GIIGYAREEA MRTGCYGIGP DHLFLGIIRH SENVAANTLR GIDVDTDQLK
     KFIDSRVFTN EHIPYEELEH ITFSRGAQNV LSLTIMEATR SGSREASSQH LLLALCRTTG
     SYGQAFLRSV GVDYSRILSY LQKNGLLGGQ PKKQQPEQND DGDDIEYSTD ENRQQPEKKK
     GEGLEEFGYD LTKAAREGKL DPVVGRDMEI SRVIEILGRR KKNNPMLIGE PGVGKSAIVE
     GIALQIAKGD IPPSLAKKKI ISLDIASVVA GTKYRGDFEK RVKNIIATAS NDPDVILFID
     EFHTIVGAGG AGGSLDAANM LKPALARGEL QCIGATTMDE FTKIVEKDGA LDRRFQKIIV
     EATDVPQSIT ILKNLRHNYE EFHKISYTDE ALEACVRLTD RYMTDRSLPD KAIDAMDEAG
     SMVRLKGGST VGEEEIATVV SKMTGIPVNK VAESEAGRIL KMKDRLRGRI IGQDDAINTI
     VGAIQRNRAG LKDPKRPIGS FLFFGPTGVG KTQLAKCLAE YLFDSEENIV RIDMSEYMEK
     FSVSRLIGAP PGYVGYEEGG QLSERVRRKP YCVVLLDEIE KAHPDIFNLL LQVLDDGRLT
     DSEGRTVSFK NTIVIMTSNV GSRDMDEYGK GLGFATAGRN VERNRQAVLE KAVKKVFPPE
     FINRVDEQIF FNTLTKEDIE KIVDIELRDL RARAEEAGYK LNVTPSAKRF VAEAGYDPAF
     GARPLKRAVM RYIEDPVSEF IISDRLLKKN KSAEPKILKV TLTPEKDNTV VVLKSEVPET
     V
//
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