ID A0A415ZS36_9BACT Unreviewed; 862 AA.
AC A0A415ZS36;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:RHO66767.1};
GN ORFNames=DW083_18430 {ECO:0000313|EMBL:RHO66767.1};
OS Parabacteroides sp. AF48-14.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=2292052 {ECO:0000313|EMBL:RHO66767.1, ECO:0000313|Proteomes:UP000283361};
RN [1] {ECO:0000313|EMBL:RHO66767.1, ECO:0000313|Proteomes:UP000283361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF48-14 {ECO:0000313|EMBL:RHO66767.1,
RC ECO:0000313|Proteomes:UP000283361};
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:RHO66767.1}.
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DR EMBL; QUDI01000048; RHO66767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A415ZS36; -.
DR Proteomes; UP000283361; 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 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.
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:RHO66767.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RHO66767.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..138
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 154..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 450..514
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 154..172
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 96575 MW; B58B4B1196DBF5CC CRC64;
MDIIEYSREE ATRLQNSYIG PEHLMLGIIR DGEGKAVQAL RELNVDEWGI KKKIEQEIKN
TFDAEETVQH DIAISKTTER VLRMSMLESR LFKKEETGTE HLLLAILKEE FNVAAKVLNE
AGITYRSVYN YLVSGTGLKR MDDFADAEDD LEHFDEISDG YTDDDEDDED DFSSRRESPR
SSGSGTGSAQ PKSPNDTPVL DNFGTDMTRA AAENRLDPIV GREKEIERLA QILSRRKKNN
PVLIGEPGVG KSAIVEGLAL RIIQRKVSRI LFDKRVISLD MASIVAGTKY RGQFEERIKA
ILNELSKNPN IILFIDEIHT IVGAGSASGS MDAANMLKPA LARGEIQCIG ATTLDEYRKN
IEKDGALERR FQKVIVDPTT AEETLQILQN IKARYEEHHN VIYTPEALQA CVKLTERYIS
DRNFPDKAID ALDEAGSRVH ISNITVPKSI EELEAKIEAT KAEKLAAVKS QNFELAASFR
DKERQYLLQL EAAKAKWEQE LQEHRETVDE DKVAEVVAMM SGVPVQRIAK AENLKLLEMA
ENLKKKVVGQ DDAVQKIVKA IQRNRVGLKD PNKPIGTFMF LGPTGVGKTH LAKKLAEYLF
DSADSLVRID MSEYLEKFAV SRLIGAPPGY VGYEEGGQLT EKVRRKPYSV VLLDEIEKAH
PDVFNLLLQV LDEGRLTDSL GRRIDFKNTI LIMTSNIGTR QLKDFGRGVG FNTQVAGEPD
KDFSRSVIQK ALNKAFAPEF LNRVDDIIMF DQLDKEAIHK IIDIELQGLY KRVASLGYSL
ELTDAAKDFI AGKGYDVQFG ARPLKRAIQK YLEDEMAEMI IRASVGEGDT IVVDFDKDKQ
EIVTSVKKSE PTTGESLPET SI
//