ID A0A4S2F178_9ACTN Unreviewed; 859 AA.
AC A0A4S2F178;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:TGY62629.1};
GN ORFNames=E5334_04265 {ECO:0000313|EMBL:TGY62629.1};
OS Coriobacteriaceae bacterium.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae.
OX NCBI_TaxID=2011094 {ECO:0000313|EMBL:TGY62629.1, ECO:0000313|Proteomes:UP000310263};
RN [1] {ECO:0000313|EMBL:TGY62629.1, ECO:0000313|Proteomes:UP000310263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM07_P-09 {ECO:0000313|EMBL:TGY62629.1,
RC ECO:0000313|Proteomes:UP000310263};
RA Navarre W., Wong E., Huang K., Tropini C., Ng K., Yu B.;
RT "Microbes associate with the intestines of laboratory mice.";
RL Submitted (APR-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:TGY62629.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SRYE01000002; TGY62629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4S2F178; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000310263; 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: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:TGY62629.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TGY62629.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 2..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 430..465
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 142..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 94051 MW; 47D66F20BF50AA8A CRC64;
MFDKFTEKAR KVMSLAQDEA RELGQMYVGT EHLLLGLIKE GDGIAAQAMA GLDVSYDETM
AIVREITRRE AEPVPGGHIP FTPRAKRVLE GAYRETISRG QTYISTEHLL LGIVREGNGV
AMEALSRMGV SGDAVRNAVN SLMNENPDPR SRPAMADVRT GSDIMGGPSG VDGSMLEEYG
RNLTKSAQEG KLDPVIGRDS EVERVMQVLA RRQKNNPLIL GDPGVGKTAI AEGLAQLIAN
GAVPEVLRNK QIWTLDMAAL VAGSKYRGEF EERLKNVVNE VMESQYDILF IDEIHTLIGA
GSAEGSIDAA SILKPPLSRG EIQVIGATTI DEYRKHIEKD SAFERRFQPV YINEPSVADT
VVILEGLRER YEKHHHVRYT DEALTSAAVL SSRYIQDRFL PDKAIDVIDE AGARTRVHRV
VVPEEILACD AELARIKEEK AAAAKAQEFE QAALLRDKEK ELGERREQLE EKWHEELDSV
CVEVGAQDIA DVVSFITGVP VSNLTEEEAS KLLRAEKVLH ERVIGQEEAV SSVARAIRRS
RSPLKDPRRP GGSFIFLGPS GVGKTELAKS LAQFLFGSED ALITFDMSEF MEKFAVSKLV
GAPPGYVGYD EGGELTKAVR RKPYSVVLFD EIEKAHPDVF NILLQILDEG RLTDGQGRKV
DFSNTVIIMT SNIGAREIAT TAPMGFGNNA GLSDSDIKQR VTAELKRQFR PEFLNRVDEI
VVFKSLSKEQ LREIVDLMVA DLRRRLVMEG MSIELTDAAR DFVAQEGTDA VYGARPLRRA
IQTLIEDPLA EELLEGGWSA GEIVLVDFDE EGHKLSFTHG TGDIPAPELS AGPKSLPSGS
ASSRRGPIAA GTGSAEAGA
//