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Database: UniProt
Entry: A0A3D9FFX9_9SPHN
LinkDB: A0A3D9FFX9_9SPHN
Original site: A0A3D9FFX9_9SPHN 
ID   A0A3D9FFX9_9SPHN        Unreviewed;       775 AA.
AC   A0A3D9FFX9;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:RED16001.1};
GN   ORFNames=DFR46_1011 {ECO:0000313|EMBL:RED16001.1};
OS   Parasphingopyxis lamellibrachiae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Parasphingopyxis.
OX   NCBI_TaxID=680125 {ECO:0000313|EMBL:RED16001.1, ECO:0000313|Proteomes:UP000256310};
RN   [1] {ECO:0000313|EMBL:RED16001.1, ECO:0000313|Proteomes:UP000256310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26725 {ECO:0000313|EMBL:RED16001.1,
RC   ECO:0000313|Proteomes:UP000256310};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
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:RED16001.1}.
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DR   EMBL; QRDP01000004; RED16001.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D9FFX9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000256310; 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:RED16001.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RED16001.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256310};
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          143..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          753..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   775 AA;  85673 MW;  B0F4BA53590FD187 CRC64;
     MPSFARELEQ TLHNALAEAA NRKHEYATLE HLLLALTDDD HAAQVMTACG VEISELQEAV
     GVYLDNELEA LRIEGTTDPS PTSGFQRVVQ RAILHVQSSG RDEVTGANVL VALFSERESY
     AVYFLQQQDM SRLDAVSFIS HGVGKGETGS ESREISGADD EEQPEQKPGG KKKNESALKQ
     FCVNLNEKAQ AGKIDPLIGR AVEVDRTVQI LCRRSKNNPL YVGEPGVGKT AIAEGLARRI
     VEEDVPEVLL PAVIYALDMG ALLAGTRYRG DFEERLKAVV NELEKLPDAV LFIDEIHTVI
     GAGATSGGAM DASNLLKPAL SSGTIRCIGS TTYKEFRNHF EKDRALLRRF QKIDVNEPST
     EDTIKILQGL RPHYEEHHNV KYTADAIKAA VELSSRYIND RKQPDKAIDV IDETGASQML
     VAPSKRRKMI TPNEIEQVIS MMARIPPKQV STNDKQALET LETDLKRVVF GQDLAIETLS
     SAIKLSRAGL REPHKPIGNY LFTGPTGVGK TEAARQLASI MGIPLERFDM SEYMERHSVS
     RLIGAPPGYV GYDQGGLLTD AVDQHPHCVL LLDEIEKAHP DLFNVLLQVM DNGKLTDHHG
     KTVDFRNVVL IMTTNAGAAD MASEGIGFGD ISREDASEEA VKKMFTPEFR NRLDAIVPFG
     YLPPAVVARV VDKFILELEL QLSDREVHIR LDDEAKNWLT ERGYDKLYGA RPMGRLIQEK
     VKQPLAEELL FGKLVNGGEV DVTVKDDTLD FLLTPAPPKR KPPKKKKKKT PEAEV
//
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