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}.
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; 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
//