GenomeNet

Database: UniProt
Entry: A0A415ZS36_9BACT
LinkDB: A0A415ZS36_9BACT
Original site: A0A415ZS36_9BACT 
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}.
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; 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
//
DBGET integrated database retrieval system