ID A0A3N2N7S8_9BACT Unreviewed; 850 AA.
AC A0A3N2N7S8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:ROT18451.1};
GN ORFNames=EEL53_12450 {ECO:0000313|EMBL:ROT18451.1};
OS Muribaculaceae bacterium Isolate-114 (HZI).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX NCBI_TaxID=2486475 {ECO:0000313|EMBL:ROT18451.1, ECO:0000313|Proteomes:UP000273368};
RN [1] {ECO:0000313|EMBL:ROT18451.1, ECO:0000313|Proteomes:UP000273368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate-114 (HZI) {ECO:0000313|Proteomes:UP000273368};
RA Clavel T., Strowig T.;
RT "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT host preference, and functional potential of this yet undescribed family.";
RL Submitted (NOV-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:ROT18451.1}.
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DR EMBL; RIBN01000029; ROT18451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2N7S8; -.
DR Proteomes; UP000273368; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:ROT18451.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ROT18451.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000273368};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 455..490
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 153..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 451..508
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 184..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 94990 MW; 98C5AFDAA8381D10 CRC64;
MNNDFSKQFR PILEIGYEEA QRFESPYISC EHLVLGSIKN KEGYAYRILS QLKVPVSKIE
EELVEYLSEP HASVETTTLF EQQYKISLAA IRQLQLAMSE ARKMNSKVIG SEHILLALIH
DKRAMDSEIL KQIKEEYLNF DISIQAIGGF DMPPQMGGVF PPEDEDDSGF PGMSSGNQGK
ESARASERPG KDKVKSDTPA LDKFGYDMTK AASEGRLDPI VGRETEIERL AQILSRRKKN
NPVLIGEPGV GKSAIVEGLA LRIIQRKVSR VLFDKRVIGL DLAGMVAGTK YRGQFEERIK
AVLDELTKNP DIILFIDEIH TIVGAGSAPG TMDAANILKP ALARGEIQCI GATTLDEYRQ
NIEKDGALER RFQKVIVEPT SPEETLEILK QVKEKYEAHH NVNYTPDALE ACVSLTERYV
SDRNFPDKAL DALDEAGSRV HITNIVVPEE IERLEREVDA LTQDKLNAAK SQDYELAASL
RDQVVNKKNE LDSAKKEWEK SLDSDRQEVD GEKVAEVVAM MTGVPTQRIA QTEGSRLINM
GNSLKGAVVG QDDAIKKVVK AIQRNRIGLK DPDKPIGVFM FLGPTGVGKT HLAKKLAEYL
FDSTDSLIRM DMSEFMEKFT VSRLVGAPPG YVGYEEGGQL TEKVRRRPYS VVLLDEIEKA
HPDVFNLLLQ VMDEGRLTDS LGRKIDFKNT IIIMTSNVGS RQLKDFGGGV GFNTEVVTKD
QAHSVISKAL NKAFSPEFLN RVDDIVMFDQ LSKESISEII DIELKDFYKR IEKLGFKLTL
ADEAKTFIAD KGYDRNFGAR PLKRAIQKYL EDELAELMLT LNAEGKFGGT IEVTHNEGDD
KLTIKYEDIV
//
