ID G8TWW4_SULAD Unreviewed; 823 AA.
AC G8TWW4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=ATPase AAA-2 domain protein {ECO:0000313|EMBL:AEW03812.1};
GN OrderedLocusNames=Sulac_0242 {ECO:0000313|EMBL:AEW03812.1};
OS Sulfobacillus acidophilus (strain ATCC 700253 / DSM 10332 / NAL).
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX NCBI_TaxID=679936 {ECO:0000313|EMBL:AEW03812.1, ECO:0000313|Proteomes:UP000005439};
RN [1] {ECO:0000313|Proteomes:UP000005439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700253 / DSM 10332 / NAL
RC {ECO:0000313|Proteomes:UP000005439};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R.,
RA Gehrich-Schroeter G., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of chromosome of Sulfobacillus acidophilus DSM
RT 10332.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEW03812.1, ECO:0000313|Proteomes:UP000005439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700253 / DSM 10332 / NAL
RC {ECO:0000313|Proteomes:UP000005439};
RX PubMed=23407703; DOI=10.4056/sigs.2736042;
RA Anderson I., Chertkov O., Chen A., Saunders E., Lapidus A., Nolan M.,
RA Lucas S., Hammon N., Deshpande S., Cheng J.F., Han C., Tapia R.,
RA Goodwin L.A., Pitluck S., Liolios K., Pagani I., Ivanova N., Mikhailova N.,
RA Pati A., Palaniappan K., Land M., Pan C., Rohde M., Pukall R., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Mavromatis K.;
RT "Complete genome sequence of the moderately thermophilic mineral-sulfide-
RT oxidizing firmicute Sulfobacillus acidophilus type strain (NAL(T)).";
RL Stand. Genomic Sci. 6:1-13(2012).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003179; AEW03812.1; -; Genomic_DNA.
DR AlphaFoldDB; G8TWW4; -.
DR STRING; 679936.Sulac_0242; -.
DR KEGG; sap:Sulac_0242; -.
DR PATRIC; fig|679936.5.peg.246; -.
DR HOGENOM; CLU_005070_4_1_9; -.
DR Proteomes; UP000005439; 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:UP000005439};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 2..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 419..454
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 415..465
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 823 AA; 91762 MW; B13731CA9CD9F8A0 CRC64;
MFGQFTEKAR RVVINAQDEA RRMGHNFVGT EHLLLGLIRE SNSLPAKILQ SIGLDLETVR
SEVLKATGRG PAIGPNEEVV FTPRAKKVVL ELAGEEARAL NQNYIGPEHL LLGLIREGEG
VAAQVLLAAG ADLNKVRHQL IQATGNTGGN SGGNEQQAQV NTPTLDLYGR DLTQMAREGK
LDPVIGRDKE AERVIQILSR RTKNNPVLIG EPGVGKTAVV EGLAQRIVEN KVPEILKDRR
VVALDLGAML AGSKYRGEFE DRLKRAMNEI REAKNVILFI DEMHTIVGAG AAEGAIDAAN
ILKPALARGE LQAIGATTLD EYRKYIERDP ALERRFQPIM VEEPSAEEAV QILKGLRDRY
EAHHRVNITD DAIEAAVHLS DRYVSDRFLP DKAIDLIDEA ASRVRLKSYV APPDLKDLAD
KLEEIRKEKE AAVQAQEFEK AAQMRDEEQK LREELERQTH EWHNRQRVET ITVTPDDIAH
IVSSWTGIPV ERLASEESER LLNLEEELHR RVVGQEEAVR AVSRAIRRAR AGLKNPRRPI
GSFLFLGPTG VGKSELAKAL AQALFGDEDA MITIDMSEYM ERHAVSRLVG APPGYVGYEE
GGQLTEAVRR HPYSVVLLDE IEKAHPEVFN ILLQVLEEGR LTEAKGRAVD FRNTVIIMTS
NVGAEVIKRQ ATIGFRKDTE ETAYRDMKDR LMDEVKHTFR PEFINRVDEI IVFHELSEKH
LAEIVGIMLK EVEDRIGQNG YRLTVSDAAK AIIAKEGFDP VFGARPLRRA IQHLVEDELA
EQILAGKFAE GAHIYVDAED GKLVFRTMTE HDSAMESIAQ KGS
//
