ID L0FRV4_ECHVK Unreviewed; 842 AA.
AC L0FRV4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=ATPase with chaperone activity, ATP-binding subunit {ECO:0000313|EMBL:AGA76659.1};
GN OrderedLocusNames=Echvi_0369 {ECO:0000313|EMBL:AGA76659.1};
OS Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Echinicola.
OX NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA76659.1, ECO:0000313|Proteomes:UP000010796};
RN [1] {ECO:0000313|Proteomes:UP000010796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC {ECO:0000313|Proteomes:UP000010796};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Echinicola vietnamensis DSM 17526.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP003346; AGA76659.1; -; Genomic_DNA.
DR RefSeq; WP_015264226.1; NC_019904.1.
DR AlphaFoldDB; L0FRV4; -.
DR STRING; 926556.Echvi_0369; -.
DR KEGG; evi:Echvi_0369; -.
DR PATRIC; fig|926556.3.peg.372; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_10; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000010796; 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 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 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; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000010796};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..152
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 443..478
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 143..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..496
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 164..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 842 AA; 94127 MW; BF84FC4943332867 CRC64;
MEAKFSNRVK EVISLSREEA LRLGHDYIGT EHLLLGMIRE GEGVAVSILK KLGVPLDELR
NSVERAVKGT ANHNVKNLAN IPLTRQSEKV LKITYLEAKI FKSQLIGTEH LLLSILRDED
NIATQILHKF DTTYDTVKEM LEFQTDQTPR SGAEADDTDE ESSKLFGSSG GSSGGGGKGS
TEKSRTPVLD NFGRDLTRMA EDDKLDPIIG REKEIERVAQ ILSRRKKNNP ILIGEPGVGK
TAIAEGLALR IVQKKVSRVL FNKRVVTLDL ASLVAGTKYR GQFEERMKAV MNELEKSPNV
ILFIDELHTI VGAGGASGSL DASNMFKPAL ARGEIQCIGA TTLDEYRQYI EKDGALARRF
QMVMVDATTP EETVQILNNI KDKYEDHHNV NYTPEAIDAC VKLSDRYISD RFLPDKAIDI
LDEAGARVHI NNIHVPDEIL KLEEEVENIK VEKNRVVKSQ KYEEAAQLRD REKKLLEQLE
NAKAKWEEES KTKRYTVEED NVAEVIAMMT GIPAKRIAQK EGNKLLNMGI ELQDKVIGQN
DAIKKLTKAI QRTRVGLKDP KKPIGSFVFL GPTGVGKTEL AKTLATYLFD KEDSLVRIDM
SEYMEKFSVS RLVGAPPGYV GYEEGGQLTE KVRRKPYSVV LLDEIEKAHP DVFNLLLQVL
DDGILTDGLG RRVDFRNTVI IMTSNIGVRD LKDFGAGIGF ASKAKQENMD EVMKSTIQSA
LKKAFSPEFL NRLDDVVVFN SLNKDDIHKI IDITLEKLFS RITELGYKIE LSDKAKDFLA
DKGYDQQYGA RPLNRAIQKY LEDAIAEEIL KGDLSEGDVI KADYPGKGDE LNISVKKKEK
AD
//
