ID R6VHW1_9FIRM Unreviewed; 852 AA.
AC R6VHW1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=ATP-dependent chaperone ClpB {ECO:0000313|EMBL:CDC82047.1};
GN ORFNames=BN746_02074 {ECO:0000313|EMBL:CDC82047.1};
OS Erysipelotrichaceae bacterium CAG:64.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=1262981 {ECO:0000313|EMBL:CDC82047.1, ECO:0000313|Proteomes:UP000018179};
RN [1] {ECO:0000313|EMBL:CDC82047.1, ECO:0000313|Proteomes:UP000018179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:64 {ECO:0000313|Proteomes:UP000018179};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, 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:CDC82047.1}.
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DR EMBL; CBGA010000014; CDC82047.1; -; Genomic_DNA.
DR AlphaFoldDB; R6VHW1; -.
DR Proteomes; UP000018179; 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; 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 78, MITOCHONDRIAL; 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; 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|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 3..143
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 395..496
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 852 AA; 97066 MW; EBF878202EAB89D5 CRC64;
MNFDKMSEKL QEIIMQAVEI CKSYQHTTVD TIQMLKAIFE HDVLDGLFKR LNIDKTRALT
LIDQEMNRVA TSSNVNPQLS NEVAQSFSRA EQWSAGIQET YLSVASVWIA LMFNKSYISK
QLVKEFHLNE KTCKDEELKR RGGKKMDSPN AEANLEALSK YGRNLVEDVK NGKIDPIIGR
DDEIRRVIQI LSRKTKNNPV LIGEPGVGKT AVVEGIAWRI MKGDVPQSLK EKKLIELDMG
SLIAGAKYRG EFEERLKSIL EEVKQAEGNI ILFIDEIHNL VGAGKTEGSM DAGNMLKPML
ARGELRCIGA TTFNEYRQYI EKDAALERRF QRVMVQEPSV EDTISILRGL KDRFESYHGV
KILDEAILAA ATMSNRYITD RFLPDKAIDL IDEACATLRV EMESMPQELD ELQRKIMQLQ
IEETALKKEE DKKAKERLED IRTELAQLQA EKDSLYTKWE DEKAELEESK DAKVRLEKAK
LDLEQAQNEA RYEDAAKLQY ATIPHLEKLI REQSDKQKED ALIQETVNEE LIAKIVSRWT
GVEVSRLVES ERQKLLHLKE ALQKRVIGQD NALELVSDAI LRSKAQIQDE HRPIGSFLFL
GPTGVGKTEV AKALAEQLFD SESHIVRIDM SEYMEKHSVS RLIGAPPGYV GYDEGGQLSE
AVRRNPYSII LFDEVEKAHP DVFNVLLQIL DDGRITDSKG VTVDFKNTLL IMTSNLGSQF
AFDGADRDTN YMNEVKKYFK PEFINRIDEI VVFNALNEDM LGKIAHKFMR ELTQRLAHKD
ITLQVSDAVY RAIATQGVDP LYGARPMKRY IQRNIETLIA RRMIEGNAGK DDTIRVDVRD
GEYTVEITHS EN
//
