GenomeNet

Database: UniProt
Entry: A0A328VHL1_9CHLR
LinkDB: A0A328VHL1_9CHLR
Original site: A0A328VHL1_9CHLR 
ID   A0A328VHL1_9CHLR        Unreviewed;       900 AA.
AC   A0A328VHL1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Clp R domain-containing protein {ECO:0000259|PROSITE:PS51903};
GN   ORFNames=A4R35_08550 {ECO:0000313|EMBL:RAQ95582.1};
OS   Thermogemmatispora tikiterensis.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Thermogemmatisporales;
OC   Thermogemmatisporaceae; Thermogemmatispora.
OX   NCBI_TaxID=1825093 {ECO:0000313|EMBL:RAQ95582.1, ECO:0000313|Proteomes:UP000248706};
RN   [1] {ECO:0000313|EMBL:RAQ95582.1, ECO:0000313|Proteomes:UP000248706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T81 {ECO:0000313|EMBL:RAQ95582.1,
RC   ECO:0000313|Proteomes:UP000248706};
RA   Tomazini A., Lal S., Stott M., Henrissat B., Polikarpov I., Sparling R.,
RA   Levin D.B.;
RT   "Analysis of Carbohydrate Active Enzymes in Thermogemmatispora T81 Reveals
RT   Carbohydrate Degradation Ability.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:RAQ95582.1}.
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DR   EMBL; MCIF01000002; RAQ95582.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328VHL1; -.
DR   Proteomes; UP000248706; 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; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248706};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..149
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          155..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          859..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..889
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   900 AA;  98239 MW;  FC7026451706CF93 CRC64;
     MYETYTPAAR LALHYAREEA SKRHRRLIGN EQLLLGILRL NDPLIGQLLT SFMLRPPLLR
     HMIEALDRPR KRVQASRQTL SPATRMALRA AALHARRLGA PSIAPEHLLL GLLSVQDRQA
     ALLLGLLEGF GITCASVRAR LLALATSGSL PDQAIFTPAQ AGEPGAQGSS ASDLPSGSSA
     SRASDLQSSY RERYERTPEL NSVSHDLTLA ALEGRLDPLI GREAELTRTI QILLRYTKNN
     PLLLGPAGSG KTAIVEGLAA RIAAGSVPEC LRGKRVVALD IGLLIAGTRY RGDLEERVQG
     IVAEIKSASD VLLFIDEIHM LIGAGGPASA PNVANLLKPL LARGHLQCIG ATTFEEYTRH
     FEQDAALARR FQPVFIAEPD AVETLAILQA LRPRYEAFHR VIISDEALKA AVRLSGRYLA
     GRTQPDKAID LIDEAAATLH MRQALPPPAL RQLHEELASL RAKREAAIRQ QHFSTALELR
     RQEQQLLRRA LAIESEWLMQ RLSGTVASNA ATPAARPRVD ERAVATVVAQ WTGLQVTFPG
     GAEAQYLLSL EHLLQQRVAG QEEAITTVAR AVRRARSNLR DPRRPAASFL FVGPSGVGKS
     HLATALAEVL TGDERALIAL DMAAFTERQQ VQRLLGSPPG YQGYKESGLL SEALRQRPAS
     IVLFEGLEKA HPALFDLLLQ VLEDGHLSDG QGRLVNFREA IIILTTNLPT SPDQAAVLGF
     GSGLPQSGLS PIRRWKQLLT QLQHSFRPEL LNRLDAIIPF HPLKREHLGQ IVDQLLGTSC
     QRLAQLGINL QISPAARDYL LSRGQRQLLI EGARPLRRLV RHEVEDRLSE ALLRGEIGRG
     DHLFLVPDGE SSYLRLERLS QARSRGQSPS IEPPPSSSST DSSPGSVARS WSEVPGHSAA
//
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