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Database: UniProt
Entry: J2PDL1_9BACL
LinkDB: J2PDL1_9BACL
Original site: J2PDL1_9BACL 
ID   J2PDL1_9BACL            Unreviewed;       712 AA.
AC   J2PDL1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=ATPase with chaperone activity, ATP-binding subunit {ECO:0000313|EMBL:EJL25322.1};
GN   ORFNames=PMI05_03910 {ECO:0000313|EMBL:EJL25322.1};
OS   Brevibacillus sp. BC25.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1144308 {ECO:0000313|EMBL:EJL25322.1, ECO:0000313|Proteomes:UP000007278};
RN   [1] {ECO:0000313|EMBL:EJL25322.1, ECO:0000313|Proteomes:UP000007278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC25 {ECO:0000313|EMBL:EJL25322.1,
RC   ECO:0000313|Proteomes:UP000007278};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJL25322.1}.
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DR   EMBL; AKIX01000068; EJL25322.1; -; Genomic_DNA.
DR   RefSeq; WP_007725101.1; NZ_AKIX01000068.1.
DR   AlphaFoldDB; J2PDL1; -.
DR   PATRIC; fig|1144308.3.peg.3861; -.
DR   Proteomes; UP000007278; 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; 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; 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; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}.
FT   DOMAIN          339..374
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          64..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          335..367
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        65..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   712 AA;  79007 MW;  CCC7BA569A1100AD CRC64;
     MHCEICKQRE ATVTVHIRVQ NQQQKYDLCQ DCKTKLTNQM GVGMGFSPFS SFSGLDEFLQ
     GFAQGQVNPG KSSSQPRPQA PERGGGILDD LGRNLNDSAR AGLIDPVIGR EQEIERVIEI
     LNRRNKNNPV LIGEPGVGKT AIAEGLALRI TEGQIPTKLK NKQVYILDVA SLVAGTGIRG
     QFEEKMKQVI AELQKRKNVI LFVDEIHLLV GAGSAEGSMD AGNILKPALA RGELQLIGAT
     TLKEYRVIEK DAALERRLQP VMVKEPTVEQ SIEILKGLRP KYEAFHQVAY SDDVIRASVE
     YSHRYIQDRF LPDKAIDLMD EVGSRLNLRS SAVDTAELHE RLAQINQEKK EATEQEAYER
     AARLRDEEAG ILEKLDQIEG KEQRVQVDVT DIQALIEQKT GIPVTKLQSD EQMKMKNLAA
     HLEAKIIGQS EAVTQVAKAI RRSRAGLKPK NRPIASFLFV GPTGVGKTEL SKALAEELFG
     TRDSMIRLDM SEYMEKHSVS KLIGSPPGYV GHEEAGQLTE RVRRNPYSII LLDEIEKAHP
     DVMHMFLQIL EDGRLTDSQG RTVNFKETVI IATSNAGVSE RKISVGFGAK APEPATVLDS
     LGAYFKPEFL NRFDSIISFA HLEKQDLVKI VDLLLQDVMG NLAEQGMEIS VTDAAKEKLA
     ELGYNPSFGA RPLRRVIQQY VEDGIADLVM EEDNVTSMLI DVEDEGIRVK KG
//
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