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Database: UniProt
Entry: A0A0F5IYI6_9BACT
LinkDB: A0A0F5IYI6_9BACT
Original site: A0A0F5IYI6_9BACT 
ID   A0A0F5IYI6_9BACT        Unreviewed;       846 AA.
AC   A0A0F5IYI6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN   ORFNames=HMPREF1536_04178 {ECO:0000313|EMBL:KKB50639.1};
OS   Parabacteroides gordonii MS-1 = DSM 23371.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=1203610 {ECO:0000313|EMBL:KKB50639.1, ECO:0000313|Proteomes:UP000033035};
RN   [1] {ECO:0000313|EMBL:KKB50639.1, ECO:0000313|Proteomes:UP000033035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS-1 {ECO:0000313|EMBL:KKB50639.1,
RC   ECO:0000313|Proteomes:UP000033035};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Martens E., Sakamoto M.,
RA   Benno Y., Suzuki N., Matsunaga N., Koshihara K., Seki M., Komiya H.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Parabacteroides gordonii DSM 23371.";
RL   Submitted (APR-2013) 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:KKB50639.1}.
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DR   EMBL; AQHW01000020; KKB50639.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F5IYI6; -.
DR   STRING; 1203610.HMPREF1536_04178; -.
DR   PATRIC; fig|1203610.3.peg.4252; -.
DR   HOGENOM; CLU_005070_4_1_10; -.
DR   Proteomes; UP000033035; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033035};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..139
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          147..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          444..508
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        147..165
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   846 AA;  95085 MW;  F414DABBCF5182A9 CRC64;
     MDVIEYSREE AARLQNSYIG PEHLMLGIIR DGEGKAMRLL HDLHADVHDI KKRIEQEIKN
     TFDTEESELH DIAISKTTER VLRMSMLESR LFKTDETGTE HLLLAILKEE FNVAAKALSE
     AGINYRNVYN NLINGTDMNR MEELEEVDEI SDGYTDDEDD DEEDFSSRKE SPRSSSGAGA
     GAAQPKSPND TPVLDNFGTD MTRAASENRL DPIVGREKEI ERLAQILSRR KKNNPVLIGE
     PGVGKSAIVE GLALRIIQRK VSRVLFDKRV ISLDMASIVA GTKYRGQFEE RIKAILNELS
     KNPNIILFID EIHTIVGAGS ASGSMDAANM LKPALARGEI QCIGATTLDE YRKNIEKDGA
     LERRFQKVIV DPTTAEETLQ ILKNIKPRYE EHHNVIYTDE ALDACVKLTE RYISDRNFPD
     KAIDALDEAG SRVHISNITV PKSIEELEAK IEDTKTEKLA AVKSQNFELA ASFRDKERQY
     LLQLEAAKAK WEQELQEHRE TVDEEKVAEV VAMMSGVPVQ RIAKAENLRL LEMAENLKKQ
     VVGQDDAVQK IVKAIQRNRV GLKDPNKPIG TFMFLGPTGV GKTHLAKKLA EYLFDSADAL
     VRIDMSEYLE KFAVSRLIGA PPGYVGYEEG GQLTEKVRRK PYSVVLLDEI EKAHPDVFNL
     LLQVLDEGRL TDSLGRRIDF KNTILIMTSN IGTRQLKDFG RGVGFSSQAA GEMDKDFSRS
     VIQKALNKAF APEFLNRVDD IIMFDQLDKD AIHKIIDIEL QGLYKRVCGL GYELVLTDEA
     KDFIATKGYD VQFGARPLKR AIQKYLEDEM AELIIRASVG EGDKIVVDFN KDEQKIVTSV
     QKKEQA
//
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