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Database: UniProt
Entry: A0A171KTW7_9BURK
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ID   A0A171KTW7_9BURK        Unreviewed;       775 AA.
AC   A0A171KTW7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:RZS70334.1};
DE   SubName: Full=Clp protease ClpX {ECO:0000313|EMBL:KKO72334.1};
GN   Name=clpA {ECO:0000313|EMBL:KKO72334.1};
GN   ORFNames=AAV32_04340 {ECO:0000313|EMBL:KKO72334.1}, EV679_1737
GN   {ECO:0000313|EMBL:RZS70334.1};
OS   Kerstersia gyiorum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Kerstersia.
OX   NCBI_TaxID=206506 {ECO:0000313|EMBL:KKO72334.1, ECO:0000313|Proteomes:UP000078084};
RN   [1] {ECO:0000313|EMBL:KKO72334.1, ECO:0000313|Proteomes:UP000078084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1 {ECO:0000313|EMBL:KKO72334.1,
RC   ECO:0000313|Proteomes:UP000078084};
RA   Greninger A.L., Kozyreva V., Chaturvedi V.;
RT   "Genome sequence of Kerstersia gyiorum CG1.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RZS70334.1, ECO:0000313|Proteomes:UP000292039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16618 {ECO:0000313|EMBL:RZS70334.1,
RC   ECO:0000313|Proteomes:UP000292039};
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 (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC       involved in the recovery of the cell from heat-induced damage, in
CC       cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC       processing of protein aggregates. Protein binding stimulates the ATPase
CC       activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC       which probably helps expose new hydrophobic binding sites on the
CC       surface of ClpB-bound aggregates, contributing to the solubilization
CC       and refolding of denatured protein aggregates by DnaK.
CC       {ECO:0000256|ARBA:ARBA00025613}.
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:KKO72334.1}.
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DR   EMBL; LBNE01000002; KKO72334.1; -; Genomic_DNA.
DR   EMBL; SGWZ01000002; RZS70334.1; -; Genomic_DNA.
DR   RefSeq; WP_068368043.1; NZ_VZPC01000005.1.
DR   AlphaFoldDB; A0A171KTW7; -.
DR   STRING; 206506.AAV32_04340; -.
DR   GeneID; 73001145; -.
DR   PATRIC; fig|206506.3.peg.940; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000078084; Unassembled WGS sequence.
DR   Proteomes; UP000292039; 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:KKO72334.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KKO72334.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078084};
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          148..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   775 AA;  84409 MW;  A15FE455282BBDA7 CRC64;
     MISQELEVSL HMAFVEARAA RHEFITVEHL LLSLLDNVSA AEVLRACNVD LELLRSNLRQ
     FVAENTPVAA EGAEVDTQPT LGFQRVIQRA IMHVSSSGGT ARKPVSGANV LVAIFGEKDS
     HAAYYLQQQG LTRLAVVNYL SHGIAPKATE EAPESPAPQQ PRTPQSETGD NRQQSPLEQY
     AHNLNAAALA GRIDPLIGRE EEVERVIQIL CRRRKNNPLL VGEAGVGKTA IAEGLAWRVT
     RGDVPEILCE TQVYALDIGA LLAGTKYRGD FEQRLKAVLK QLKGNPNAVL FIDEIHTLIG
     AGSASGGTLD ASNLLKPALS SGQLKCMGAT TYTEYRGIFE KDSALSRRFQ KVDVAEPTVA
     QTVQILRGLK SRFESHHGVR YANTALVAAA ELSARHISDR HLPDKAIDVI DEAGAAQRLL
     PKSKQKKVIS RTDIEAIVAR MARIPPQSVS TDDRNRLASL ERDLQAVVFG QDPAIEALAA
     AIKMSRSGLG KTDKPIGSFL FSGPTGVGKT EVARQLAFTL GVELLRFDMS EYMERHAVSR
     LIGAPPGYVG FDQGGLLTEA VSKHPHCVLL LDEIEKAHPD VFNILLQVMD HGALTDNNGR
     KADLRNVILI MTTNAGAESL SKRSIGFAQS ETRGDEMAEI KRLFSPEFRN RLDAIVSFAP
     LSRDIILRVV DKFLLQLEQQ LHEKRVEATF TDTLREHLAA EGFDPLMGAR PMQRLIQDTI
     RKALADELLF GKLTQGGSVV VDLDGNGNVV LNFPKQDDAQ ASGAGSDRPE EALAD
//
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