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Database: UniProt
Entry: A0A3Q8T973_9RICK
LinkDB: A0A3Q8T973_9RICK
Original site: A0A3Q8T973_9RICK 
ID   A0A3Q8T973_9RICK        Unreviewed;       770 AA.
AC   A0A3Q8T973;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:AZL15917.1};
GN   Name=clpA {ECO:0000313|EMBL:AZL15917.1};
GN   ORFNames=EF513_05100 {ECO:0000313|EMBL:AZL15917.1};
OS   Rickettsiales endosymbiont of Stachyamoeba lipophora.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX   NCBI_TaxID=2486578 {ECO:0000313|EMBL:AZL15917.1, ECO:0000313|Proteomes:UP000267655};
RN   [1] {ECO:0000313|EMBL:AZL15917.1, ECO:0000313|Proteomes:UP000267655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RICK01 {ECO:0000313|EMBL:AZL15917.1,
RC   ECO:0000313|Proteomes:UP000267655};
RA   Munoz-Gomez S.A., Hess S., Burger G., Lang B.F., Susko E., Slamovits C.H.,
RA   Roger A.J.;
RT   "An updated phylogeny of the Alphaproteobacteria reveals that the parasitic
RT   Rickettsiales and Holosporales have independent origins.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP033611; AZL15917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q8T973; -.
DR   KEGG; ren:EF513_05100; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000267655; 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:AZL15917.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AZL15917.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267655};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..67
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
SQ   SEQUENCE   770 AA;  86259 MW;  917E9312157CB0D6 CRC64;
     MISRSLELCL NRTIEYARDF KHQFALIEHL LLALLDDPDV YSIIRGCGVN PEVVINKLKN
     YLSHTKGLNI QNLQLPFEIG LSESLQKIVH RATINAHNAG QKEVCGIHVF AEIFNEQDSF
     AVICMNEHHI TKLDVLNYLM HGVTKQQTAS NQQYHLNLND NSQNEPNNNS GKTHKFEIIN
     PTPSIKEAKP SNNPLDLYCV NVNKQAIQGE IDPLIGRENE VGRAIEILSR RSKNNPLFIG
     DPGVGKTAMV EGLAQRIVNK QVPHSLHKAV IYSLDMGALL AGTRYRGDFE ERIKSVIREI
     EKLPESILFI DEIHTIIGAG ATSGGSLDAS NLLKPALSRG NFRCIGSTTF KEYSNHFEKD
     HALVRRFQKI VVESTSIPES IKILYGLKGH YEKFHKINYK DGTIEAAVQL ADRYINQKQL
     PDKAIDVMDE AGAHVKLNSN KKRKYVTIDD IERIVAKIAN VPIQSLTQDE SHKLQNLESN
     LKQTIYGQDK AIEALCSAIK LSRAGLRQTK KPIGCYLFSG PTGVGKTELA KKLSSFIDME
     LIRIDMSEYM ERHSISKLIG TPPGYVGFDQ GGILTDAVTK TPYSVVLFDE IEKADSDIYN
     ILLQVMDYGN LTDHTGKQIS FCNTIIIMTS NVGAKELTKA PMGFSRDISG NDSKEAINRV
     FTPEFLNRLD AIIPFEPLTN DTINHVVNKF IEQLKEQLLT KHVEIDLSDN AVSFLIEKGF
     DQLNGARPLE RVIDNNIKKN LADEILFGRL NKGGKVYIDC KNGEIDFEIN
//
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