ID Q5FGX6_EHRRG Unreviewed; 764 AA.
AC Q5FGX6;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpA {ECO:0000313|EMBL:CAI27930.1};
GN Name=clpA {ECO:0000313|EMBL:CAI27930.1};
GN OrderedLocusNames=ERGA_CDS_04780 {ECO:0000313|EMBL:CAI27930.1};
OS Ehrlichia ruminantium (strain Gardel).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=302409 {ECO:0000313|EMBL:CAI27930.1, ECO:0000313|Proteomes:UP000000533};
RN [1] {ECO:0000313|EMBL:CAI27930.1, ECO:0000313|Proteomes:UP000000533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gardel {ECO:0000313|EMBL:CAI27930.1,
RC ECO:0000313|Proteomes:UP000000533};
RX PubMed=16547041; DOI=10.1128/JB.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(2006).
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; CR925677; CAI27930.1; -; Genomic_DNA.
DR RefSeq; WP_011255602.1; NC_006831.1.
DR AlphaFoldDB; Q5FGX6; -.
DR KEGG; erg:ERGA_CDS_04780; -.
DR HOGENOM; CLU_005070_4_2_5; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000000533; 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: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; 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 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; 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:CAI27930.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CAI27930.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 218..363
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 498..641
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 666..757
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 764 AA; 85884 MW; 46643CDE03483686 CRC64;
MLSKNLEDSL HKALSIAFDF HHEYATLEHL LLALTDDIDA RRVFYAFRVS IDKLKITIIN
FLRYEIPTLI DKGISEVKPT IIFERLVHRA IIHAHSSGIS EITGADILSE ILAEKDSYSA
SFLHEQNIKY IDVVNYISNN NSGSYVNDFS MDQEFRDYEY NKPINSFVTV PKDILKDNEI
LNAYCINLNE SAKKGKIDYV IGRSYELSRT MEVLLRRRKN NPLYVGDPGV GKTAIVEGLA
LNIIDGNVPE QLKKMVIYSL DMGSLLAGTR YRGDFEERIK SVIKAIEAKE NAILFIDEIH
TIVGAGSTSG GSLDASNLLK PALARGTLRC IGATTYKEYN NNFEKDRALA RRYQKINVEE
SSVDETVRIL RGIQSYYASY HNVTYSEDSI DRAAELSDRY ISEKMLPDKA VDVIDEAGAY
CNLHNSNGNR VITGSDIEHI VSRITGIPSR NLAHNDLDKV KNLEKNLKQH IFGQDFAISS
LVDSIKIAKA GLRDHRKPLA SYLFTGPTGV GKTELAKQLA NHMGMKLIRF DMSEYMESHS
ISKIIGSPPG YVGYDQGGLL TDSISRHQYS VLLLDEIEKA HSDIYNILLQ IMDYGCVTDT
YGRKVSFHNV IVILTTNAGA FELSRNSIGF SRNRSFNQGD DKQAIERIFS PEFRNRLDAI
ISFSSLNQSA VLQVVNKFIN ELKEQLAKKG IHFNIGDDVL LYLAKSGYDS IPGVRNIESI
ISQKIKRYLS DEILFGRLSN GGYVKIILDP NTNDLIYDFC CAEV
//