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Database: UniProt
Entry: F2JMX0_CELLD
LinkDB: F2JMX0_CELLD
Original site: F2JMX0_CELLD 
ID   F2JMX0_CELLD            Unreviewed;       737 AA.
AC   F2JMX0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=ATPase AAA-2 domain protein {ECO:0000313|EMBL:ADZ85885.1};
GN   OrderedLocusNames=Clole_4213 {ECO:0000313|EMBL:ADZ85885.1};
OS   Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS   RHM5) (Clostridium lentocellum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC   Cellulosilyticum.
OX   NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ85885.1, ECO:0000313|Proteomes:UP000008467};
RN   [1] {ECO:0000313|EMBL:ADZ85885.1, ECO:0000313|Proteomes:UP000008467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC   {ECO:0000313|Proteomes:UP000008467};
RX   PubMed=21398547; DOI=10.1128/JB.00239-11;
RG   US DOE Joint Genome Institute;
RA   Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA   Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA   Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA   Angert E.R., Currie C.R.;
RT   "Complete genome sequence of the cellulose-degrading bacterium
RT   Cellulosilyticum lentocellum.";
RL   J. Bacteriol. 193:2357-2358(2011).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP002582; ADZ85885.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2JMX0; -.
DR   STRING; 642492.Clole_4213; -.
DR   KEGG; cle:Clole_4213; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_9; -.
DR   Proteomes; UP000008467; Chromosome.
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   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:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 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; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008467};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..130
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          131..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..150
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   737 AA;  82506 MW;  C498F00B87A81B5A CRC64;
     MKAKELACNY KHEYITPEHI LLVMCDVSVF CEAFEACNGD IQVLKTNLEG YLEENLEKKE
     DIEPIESFSL QQVYIRSSEQ VINSGKEQIE LDHLLSGIMG LPESYGVYYI LEQGVTLRDL
     LFELCHAQDD DSTQLEKPSD EEEEEQTTSE EKDIESIAKY VTNLNKVVAA SNEPLIGREE
     ILKRTIQVLC RKNKNNPIHI GEPGVGKTAI TMGIAQLLNE GKVPKVLEGA QIFSLDLGAT
     LAGTQYRGDF EKRLKKILDI LKKQYKPIVY IDEIHNIVGA GSLGAGSLDA SNLLKPYLTE
     GSIKFIGATT FEEYKKYVEK DKGLVRRFQA IEVLEPSIEE AITILRGLKS SYEAYHGVTY
     TDEAIRGAVQ LSQQYMNDRF LPDKAIDLLD EAGAYYTVYD SGSKNRKKKP IIDLSIIEQT
     LSKICHIPQQ KIEKNEVQVL GQLEQNLKKQ VFGQDKAIEQ VVMSIKLSRA GLSEMNKPIA
     SLLFVGPTGV GKTEIAKCLA NELGIKLIRF DMSEYTEKHT ASKLIGSPPG YIGYEEGGLL
     TDAIRKSPYC VLLLDEIEKA HQDIYNILLQ VMDYATLTDN KGRKADFRNV ILIMTSNAGA
     SRIGKNLVGF GERKIQGEAI NDEVKKVFSP EFRNRLSSII AFNHITEDMA LLIVRKELSK
     LKKVAKEKGI KLSFNQKCIE YIVTKGVSAE YGAREISRLI ESKIKPLLAQ EILFGSLNEG
     GSCKISLVEE EFKIKVN
//
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