ID A0A371R8J2_9PROT Unreviewed; 779 AA.
AC A0A371R8J2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:RFB01764.1};
GN Name=clpA {ECO:0000313|EMBL:RFB01764.1};
GN ORFNames=DX908_14260 {ECO:0000313|EMBL:RFB01764.1};
OS Parvularcula marina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC Parvularculaceae; Parvularcula.
OX NCBI_TaxID=2292771 {ECO:0000313|EMBL:RFB01764.1, ECO:0000313|Proteomes:UP000264589};
RN [1] {ECO:0000313|EMBL:RFB01764.1, ECO:0000313|Proteomes:UP000264589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1705 {ECO:0000313|EMBL:RFB01764.1,
RC ECO:0000313|Proteomes:UP000264589};
RA Sun L.;
RT "Parvularcula sp. SM1705, isolated from surface water of the South Sea
RT China.";
RL Submitted (AUG-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFB01764.1}.
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DR EMBL; QUQO01000002; RFB01764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371R8J2; -.
DR InParanoid; A0A371R8J2; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000264589; Unassembled WGS sequence.
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:RFB01764.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RFB01764.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000264589};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 144..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 86583 MW; 657CD74589F6F322 CRC64;
MATFSENLER SIHRAIALAT EKKQELATLE HLLYSLTEDP DAKAVMEACD VDIEELREQL
IEYIDEDLEK LRVEDADDAK PTAGFHRVVQ RALIHVETSG RSEVTGANIL VAIFAERESH
ATFFLNTHGM TRYDAVNYIS HGLPKNGAPA PGRSPRGVEE DEESATKQGP QALEAYTVDL
NAKARKGKID ILVGREKEVE RAIQVLCRRR KNNPLFVGDP GVGKTAIAEG LARRIVDEEV
PEVLAEATIF SLDMGALLAG TRYRGDFEER MKAVLKELEA HHDAILFIDE IHTIIGAGAT
SGGAMDASNL LKPALQAGSL KCMGSTTFKE YKQHFEKDRA LSRRFQKIDI VEPSIQDTIE
ILRGLRPAFE DHHNLTYSDE AIVTAVELSA KYMTDRRLPD KAIDVIDEAG ARQMLYKPED
RVKQIGVHEV EEIVAQMARI PSKTVSKSDT ERLKNMNEDL KRVVYGQDNA IEQLTAAIKL
SRAGLREPDK PIGSYLFAGP TGVGKTEVAK QLAKMMGVEL LRFDMSEYME RHTVSRLIGA
PPGYVGFDQG GGLLTDAVDQ NPHAVVLLDE IEKAHPEIFN ILLQVMDNGS LTDTHGKKID
FRNVIIIMTT NAGASDAAKN EIGFGRGKAT DQQNQAIEKL FTPEFRNRLD AIITFAGLSK
PIVDRIVAKF VMQLEAQLAD RNVTFELTEE ATRWLSERGF DEEMGARPLS RTIQEHIKKP
IADEILFGLL KEGGIVRVMT KKEGEKKVLD FEFIPEEPKR DPSTDGGGDG EKAEEERVR
//