ID A0A374V8Y9_9BACE Unreviewed; 842 AA.
AC A0A374V8Y9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:RGM46910.1};
GN ORFNames=DXC10_11110 {ECO:0000313|EMBL:RGM46910.1};
OS Bacteroides sp. OM08-11.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=2292284 {ECO:0000313|EMBL:RGM46910.1, ECO:0000313|Proteomes:UP000262405};
RN [1] {ECO:0000313|EMBL:RGM46910.1, ECO:0000313|Proteomes:UP000262405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM08-11 {ECO:0000313|EMBL:RGM46910.1,
RC ECO:0000313|Proteomes:UP000262405};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RGM46910.1}.
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DR EMBL; QSTJ01000005; RGM46910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A374V8Y9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000262405; 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:RGM46910.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RGM46910.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000262405};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 450..485
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 148..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 442..492
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 170..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 842 AA; 94030 MW; BB8F00730FD4839D CRC64;
MNNQFSQRVS DIITYSKEEA NRLRNRYIGP EHLLLGMLRD GGGKAIEIMM KLDIDLKQVK
SRLESFLKDA EDDTLLPDAD VPLSPMAAKI LKMCILEARL LKSATADTEH VLLAILKDGD
NLAATVLEEN QINYQSVFEL LSMKSTNPNA GMGFTEDDEE DEEDMNMSRS SRDSANGPSS
SAQTTSKKPS NDTPVLDNFG MDMTHAAEEG KLDPVVGRER EIERLAQILS RRKKNNPVLI
GEPGVGKSAI VEGLALRIVQ KKVSRILFDK RVVMLDMASV VAGTKYRGQF EERIRSIINE
LQKNPNVILF IDEIHTIVGA GAAAGSMDAA NMLKPALARG EIQCIGATTL DEYRKNIEKD
GALERRFQKV IVEPTTAEET LQILKNIKEK YEDHHNVNYT DEALEACVKL ADRYITDRNF
PDKAIDALDE AGSRVHLTNI NVPKEIEEQE KLIEEARNLK AEAVKSQNFE LAASYRDREK
ELSARLDEMK DEWKARLKDN RQTVGEEEIA NVVSMMSGVP VQRMAQAEGL KLAGMKEELQ
AKVIAQDAAI EKLTKAILRS RVGLKDPNRP IGTFMFLGPT GVGKTHLAKQ LAQYMFGSSD
ALIRIDMSEY MEKYTVSRMI GAAPGYVGYE EGGQLTEKVR RKPYSIVLLD EIEKAHPDVF
NILLQVLDEG RLTDNYGRTI DFKNTVIIMT SNIGTRQLKE FGHGVGFTAQ SRTDNNEHSR
GVIQKALNKT FAPEFLNRLD EIITFDQLSL DAITKIVDIE LKGLFERVEA IGYKLVVDED
AKKFLASKGY DVQFGARPLK RAIQNYLEDG LSELIVSSGI QPGDTVNISV DKEKDELSIK
RA
//