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Database: UniProt
Entry: A0A3A3E0C4_9RHOB
LinkDB: A0A3A3E0C4_9RHOB
Original site: A0A3A3E0C4_9RHOB 
ID   A0A3A3E0C4_9RHOB        Unreviewed;       774 AA.
AC   A0A3A3E0C4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-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:RJE81643.1};
GN   Name=clpA {ECO:0000313|EMBL:RJE81643.1};
GN   ORFNames=DWB67_03180 {ECO:0000313|EMBL:RJE81643.1};
OS   Paracoccus sp. JM45.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=2283626 {ECO:0000313|EMBL:RJE81643.1, ECO:0000313|Proteomes:UP000265822};
RN   [1] {ECO:0000313|EMBL:RJE81643.1, ECO:0000313|Proteomes:UP000265822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JM45 {ECO:0000313|EMBL:RJE81643.1,
RC   ECO:0000313|Proteomes:UP000265822};
RA   Gutierrez-Barranquer J.A., Parages M.L., Reen F.J., Ogara F.;
RT   "Draft genome sequence of Paracoccus sp. JM45.";
RL   Submitted (JUL-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:RJE81643.1}.
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DR   EMBL; QQVY01000001; RJE81643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A3E0C4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000265822; 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:RJE81643.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RJE81643.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          150..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          755..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   774 AA;  85102 MW;  027DB7204974B0BA CRC64;
     MPSFSTSLEQ AIHQALALAN EHKHELATLE HLLLALTEEP EAVKVMRACN VDLEELRKSL
     VEFIEDDLST LITEIEGSEA VPTAAFQRVI QRAAIHVQSS GRQEVTGANV LVAIFAERES
     NAAYFLQELD MTRYDAVNYI AHGVAKNPSF NEPRKVEGSD DPIDNDKVEG SAEAKDETAL
     GKYCVDLNVK SKKGDVDPLI GRDTEVERAI QVLCRRRKNN PLLVGDPGVG KTAIAEGLAL
     KITRGQTPDV LSGATIFSLD MGALLAGTRY RGDFEERLKA VVKELEAHPD AILFIDEIHT
     VIGAGATSGG AMDASNLLKP ALAGGKLRCM GSTTYKEYRQ HFEKDRALAR RFQKIDVNEP
     TVPDAIKILM GLKPHFEKHH DLRYTNDAIK SAVELASRYI NDRKLPDSAI DIIDEAGAAQ
     HLVAESKRRK TISPKEIEAV VAKIARIPPK NVSKNDAEVL RDMETSLKRV VFGQDTAINT
     LSSAIKLARA GLREPEKPIG NYLFAGPTGV GKTEVAKQLA STLGVELLRF DMSEYMEKHA
     VSRLIGAPPG YVGFDQGGLL TDGVDQHPHC VLLLDEIEKA HPDVFNILLQ IMDAGRLTDH
     NGRQVDFRNV ILIMTSNAGA ADQAKAAIGF GRDRREGEDT AAIERTFTPE FRNRLDAIIS
     FAPLSRDVVI HVVEKFVLQL EAQLMDRNVH IELTPQAADW LAERGYDDRM GARPLGRVIQ
     EHIKKPLAEE LLFGRLTKGG FVRVKIEDDK PAFDITGPDA PRISKSKTPL LTAE
//
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