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Database: UniProt
Entry: A0A126RKA5_9SPHN
LinkDB: A0A126RKA5_9SPHN
Original site: A0A126RKA5_9SPHN 
ID   A0A126RKA5_9SPHN        Unreviewed;       772 AA.
AC   A0A126RKA5;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:AMK22466.1};
GN   ORFNames=K426_07595 {ECO:0000313|EMBL:AMK22466.1};
OS   Sphingobium sp. TKS.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1315974 {ECO:0000313|EMBL:AMK22466.1, ECO:0000313|Proteomes:UP000060779};
RN   [1] {ECO:0000313|Proteomes:UP000060779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TKS {ECO:0000313|Proteomes:UP000060779};
RA   Tabata M.;
RT   "Whole genome sequence of gamma-HCH degrading bacterium Sphingobium sp.
RT   TKS.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMK22466.1, ECO:0000313|Proteomes:UP000060779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TKS {ECO:0000313|EMBL:AMK22466.1,
RC   ECO:0000313|Proteomes:UP000060779};
RX   PubMed=27056231;
RA   Tabata M., Ohhata S., Kawasumi T., Nikawadori Y., Kishida K., Sato T.,
RA   Ohtsubo Y., Tsuda M., Nagata Y.;
RT   "Complete Genome Sequence of a gamma-Hexachlorocyclohexane Degrader,
RT   Sphingobium sp. Strain TKS, Isolated from a gamma-Hexachlorocyclohexane-
RT   Degrading Microbial Community.";
RL   Genome Announc. 4:0-0(2016).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP005083; AMK22466.1; -; Genomic_DNA.
DR   RefSeq; WP_066555647.1; NZ_CP005083.1.
DR   AlphaFoldDB; A0A126RKA5; -.
DR   STRING; 1315974.K426_07595; -.
DR   KEGG; spht:K426_07595; -.
DR   PATRIC; fig|1315974.3.peg.1588; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000060779; Chromosome 1.
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:AMK22466.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AMK22466.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000060779};
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          147..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   772 AA;  85086 MW;  AF0CE2258A964873 CRC64;
     MPSFAPALET TLHNALTHAS ERRHEYATLE HLLLALIDDE HASKVMQACG VELGELSDAV
     TQYLDSELDS LKVEGASDPS PTSGFQRVVQ RAILHVQSSG KDEVTGANVL VALFSERESY
     AVYFLQQQDM SRLDAVSYIS HGVGKGTAIP EQRETKGAQE EEKKVQDSKG KKDSALEQFT
     VNLNEKAARG KVDPLIGRAS EVDRTIQILC RRSKNNPLYV GDPGVGKTAI AEGLARKIVE
     GEVPDVLKEA VIYSLDMGAL LAGTRYRGDF EERLKAVVTE LEKMPHAVLF IDEIHTVIGA
     GATSGGAMDA SNLLKPALSG GTIRCIGSTT YKEFRNHFEK DRALLRRFQK IDVNEPTIED
     TIKILAGLRS AFEEHHNVKY TPDAIKAAVE LSARYINDRK LPDKAIDVID EVGAMQMLVV
     PSKRKKTITP KEIEQVIATM ARIPPKTVSA DDKSVLETLD TDLKRVVFGQ NRAIEVLSSA
     IKLSRAGLRD PDKPIGNYLF SGPTGVGKTE VARQLAHLLG IPLQRFDMSE YMERHSVSRL
     IGAPPGYVGY DQGGLLTDAV DQNPHCVLLL DEVEKAHPDL FNILLQVMDN GRLTDHHGKS
     VDFRNTILIM TTNAGASDMA KESIGFGEFT REDVQEDAVK KLFTPEFRNR LDAIVPFGYL
     PPEIVARVID KFVLQLELQL ADRDVHITLD DEAKAWLTKR GYDKLYGARP MGRLMQEKIK
     QPLAEELLFG KLVHGGEVHV RLKDDALAFE ITPAAPKKGK KGSKAKPAES TK
//
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