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Database: UniProt
Entry: S6HIN6_9PSED
LinkDB: S6HIN6_9PSED
Original site: S6HIN6_9PSED 
ID   S6HIN6_9PSED            Unreviewed;       756 AA.
AC   S6HIN6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=ATP-dependent Clp protease, ATP-binding subunit ClpA {ECO:0000313|EMBL:EPJ87443.1};
GN   ORFNames=CFII64_07837 {ECO:0000313|EMBL:EPJ87443.1};
OS   Pseudomonas sp. CFII64.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=911242 {ECO:0000313|EMBL:EPJ87443.1, ECO:0000313|Proteomes:UP000014850};
RN   [1] {ECO:0000313|EMBL:EPJ87443.1, ECO:0000313|Proteomes:UP000014850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFII64 {ECO:0000313|EMBL:EPJ87443.1,
RC   ECO:0000313|Proteomes:UP000014850};
RA   Feris K.P., Lalor S.J.;
RL   Submitted (NOV-2010) 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:EPJ87443.1}.
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DR   EMBL; ATLO01000012; EPJ87443.1; -; Genomic_DNA.
DR   RefSeq; WP_020290218.1; NZ_ATLO01000012.1.
DR   AlphaFoldDB; S6HIN6; -.
DR   PATRIC; fig|911242.4.peg.1566; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000014850; 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:EPJ87443.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EPJ87443.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          145..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   756 AA;  83484 MW;  9F2DE63A77B1AB26 CRC64;
     MLNRELEVTL NLAFKEARSK RHEFMTVEHL LLALLDNEAA ATVLRACGAN LDKLKHDLQE
     FIDSTTPLIP VHDEDRETQP TLGFQRVLQR AVFHVQSSGK REVTGANVLV AIFSEQESQA
     VFLLKQQSVA RIDVVNYIAH GISKVPGHGD HSEGEQDMQD DEGGESSSSG NPLDAYASNL
     NELARQGRID PLVGRELEVE RVAQILARRR KNNPLLVGEA GVGKTAIAEG LAKRIVDNQV
     PDLLANSVVY SLDLGALLAG TKYRGDFEKR FKALLNELKK RPHAILFIDE IHTIIGAGAA
     SGGVMDASNL LKPLLSSGDI RCIGSTTFQE FRGIFEKDRA LARRFQKVDV SEPSVEDTIG
     ILRGLKGRFE QHHNIEYSDE ALRAAAELAS RYINDRHMPD KAIDVIDEAG AYQRLQPVEK
     RVKRIEVAQV EDIVAKIARI PPKHVNSSDK ELLRNLERDL KLTVFGQDAA IDSLSTAIKL
     SRAGLKSPDK PVGSFLFAGP TGVGKTEAAR QLAKALGIEL VRFDMSEYME RHTVSRLIGA
     PPGYVGFDQG GLLTEAITKQ PHCVLLLDEI EKAHPEVFNL LLQVMDHGTL TDNNGRKADF
     RNVIVIMTTN AGAETAARAS IGFTHQDHSS DAMEVIKKSF TPEFRNRLDT IIQFGRLSHE
     VIKSVVDKFL TELQAQLEDK RVLLEVTDEA RSWLAAGGYD AQMGARPMAR LIQDKIKRPL
     AEEILFGELA EHGGVVHIDV KDGEMTFDFE TTAEMA
//
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