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Database: UniProt
Entry: Q0BRA3_GRABC
LinkDB: Q0BRA3_GRABC
Original site: Q0BRA3_GRABC 
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
//
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