ID Q0BRA3_GRABC Unreviewed; 851 AA.
AC Q0BRA3;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 104.
DE SubName: Full=ATP-dependent clp protease ATP-binding subunit clpA {ECO:0000313|EMBL:ABI62649.1};
GN OrderedLocusNames=GbCGDNIH1_1751 {ECO:0000313|EMBL:ABI62649.1};
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI62649.1, ECO:0000313|Proteomes:UP000001963};
RN [1] {ECO:0000313|EMBL:ABI62649.1, ECO:0000313|Proteomes:UP000001963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963};
RX PubMed=17827295; DOI=10.1128/JB.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP000394; ABI62649.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0BRA3; -.
DR STRING; 391165.GbCGDNIH1_1751; -.
DR KEGG; gbe:GbCGDNIH1_1751; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_5; -.
DR OMA; GRVIQEH; -.
DR Proteomes; UP000001963; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0043335; P:protein unfolding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR013461; ClpA.
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 NCBIfam; TIGR02639; ClpA; 1.
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 Hydrolase {ECO:0000313|EMBL:ABI62649.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ABI62649.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001963};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 64..209
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 209..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 93300 MW; 28A19830D435B9EE CRC64;
MLDGTKQDVK SSYPGWAAES SCRLVFRHCN PISSSSMPRK GACAVDRIGF RSLPAAPRIK
ERCPSMLSRN LEQTLHRALS LASERHHEYA TLEHLLLGLA EDADAVAVLR ACGVDIDKLR
TDLTEFLDKD LSGLASERAS DPKPTAGFQR VVQRAAIHVQ SSGRDEVTGA NVLVALFSER
ESHAVYFLQL QDMTRLDAVN FISHGIAKAP GRSQTRPVQG SASGSNGGGE PSGPESEREE
KSSRRKEDAL STYCVDLNKK ARAGKIDPLI GRDTEIERTI QILCRRTKNN PLYVGDPGVG
KTAIAEGLAK RIVESDVPEV LLNSTIYALD MGALLAGTRY RGDFEERLKA VVTELENHPG
AVLFIDEIHT VIGAGATSGG AMDASNLLKP ALASGALRCI GSTTYKEFRN YFEKDRALVR
RFQKIDVNEP SVEDAVKILR GLKTNYETHH KVTYTEEAIR GAVELAAKYI HDRKLPDKAI
DVIDEVGASR MLLPEHKRRK TVTLQDVEDI VARIARIPPK SVSADDKETL RTLERDLKAM
VFGQDKAIEA LSAAIKLSRA GLRDAEKPIG NYLFSGPTGV GKTEVARQLA TTLGIELIRF
DMSEYMERHS ISRLIGAPPG YVGFDQGGLL TDAIDQHPHA VLLLDEVEKA HPDLYNILLQ
VMDHGKLTDH NGKIVDFRNV ILIMTTNAGA SDMAKEAIGF GREARVGEDE DAVKRLFTPE
FRNRLDAVIP FGNLTAEIVG RVVEKFVMQL EAQLADRNVT IELNSAAKEW LAERGYDRLY
GARPLARVIQ EYIKKPLAEE LLFGKLVKGG SVKVTLKDDA LEFDIVEASA PALPRPDAND
GGEELAAETA D
//