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Database: UniProt
Entry: E6NQH5_HELPQ
LinkDB: E6NQH5_HELPQ
Original site: E6NQH5_HELPQ 
ID   E6NQH5_HELPQ            Unreviewed;       856 AA.
AC   E6NQH5;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574};
GN   Name=clpB {ECO:0000313|EMBL:BAJ59391.1};
GN   OrderedLocusNames=HPF57_0317 {ECO:0000313|EMBL:BAJ59391.1};
OS   Helicobacter pylori (strain F57).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=866346 {ECO:0000313|EMBL:BAJ59391.1, ECO:0000313|Proteomes:UP000008082};
RN   [1] {ECO:0000313|EMBL:BAJ59391.1, ECO:0000313|Proteomes:UP000008082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F57 {ECO:0000313|EMBL:BAJ59391.1,
RC   ECO:0000313|Proteomes:UP000008082};
RX   PubMed=21575176; DOI=10.1186/1471-2180-11-104;
RA   Kawai M., Furuta Y., Yahara K., Tsuru T., Oshima K., Handa N.,
RA   Takahashi N., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.;
RT   "Evolution in an oncogenic bacterial species with extreme genome
RT   plasticity: Helicobacter pylori East Asian genomes.";
RL   BMC Microbiol. 11:104-104(2011).
RN   [2] {ECO:0000313|EMBL:BAJ59391.1, ECO:0000313|Proteomes:UP000008082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F57 {ECO:0000313|EMBL:BAJ59391.1,
RC   ECO:0000313|Proteomes:UP000008082};
RX   PubMed=21212362; DOI=10.1073/pnas.1012579108;
RA   Furuta Y., Kawai M., Yahara K., Takahashi N., Handa N., Tsuru T.,
RA   Oshima K., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.;
RT   "Birth and death of genes linked to chromosomal inversion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:1501-1506(2011).
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; AP011945; BAJ59391.1; -; Genomic_DNA.
DR   RefSeq; WP_001048014.1; NC_017367.1.
DR   AlphaFoldDB; E6NQH5; -.
DR   KEGG; hex:HPF57_0317; -.
DR   PATRIC; fig|866346.4.peg.342; -.
DR   HOGENOM; CLU_005070_4_0_7; -.
DR   Proteomes; UP000008082; Chromosome.
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: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; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; 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   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:BAJ59391.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:BAJ59391.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          4..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          409..489
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   856 AA;  96551 MW;  361FA2A33E729369 CRC64;
     MNLFEKMTDQ LHETLDSALA LALHHKNAEV TPLHMLFVML NNSQGILIQA LQKMSVDIQA
     LRLSVQSELN KLAKVSQINK QNIQLNQALI QSLENAQGLM AKIGDSFIAT DVYLLANMSL
     FESVLKPYLD TKELQKTLEA LRKGATIQGK NDDSNWESLE KFGIDLTQKA LENKLDPVIG
     RDEEIIRMMQ ILIRKTKNNP ILLGEPGVGK TAVVEGLAQR IVNKEVPKTL LNKRVVALDL
     SLLVAGAKYR GEFEERLKKV IEEVKKSANV ILFIDEIHTI VGAGASEGGM DAANILKPAL
     ARGELHTIGA TTLKEYRKYF EKDMALQRRF QPILLNEPSI NEALQILRGL KETLETHHNI
     TINDSALIAS AKLSSRYITD RFLPDKAIDL IDEGAAQLKM QMESEPAKLS SVKRSIQRLE
     MERQALEMEK KESNAKRMQE ILKELSDLKE EKIQLEAQFE NEKEVFREIS RLKMETESLK
     KEAERFKRNG DYQQAGEIEY SKIPENKKKE EELQHKWEAM QQNGALLQNA LTENNIAEIV
     SQWTHIPVQK MLQSEKNRVL NIESELQKRV VGQEKAIKAI AKAIKRNKAG LSDSNKPIGS
     FLFLGPTGVG KTESAKALAQ FLFDSDKNLI RIDMSEYLEK HAISRLIGAA PGYVGYEEGG
     QLTEAVRRKP YSVVLLDEVE KAHPDVFNLL LQVLDEGHLT DSKGVRVDFK NTILILTSNV
     ASGALLEEDL SEADKQKAIK ESLRQFFKPE FLNRLDEIIS FNALDSHAVV NIVGILFENI
     QKKALERGIN VTLDEEAKEL IAEVGFDRFY GARPLKRALY EMVEDKLAEL ILEDKIKEND
     SVAFVVENNE IVPKIK
//
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