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Database: UniProt
Entry: A0A268TAF7_9HELI
LinkDB: A0A268TAF7_9HELI
Original site: A0A268TAF7_9HELI 
ID   A0A268TAF7_9HELI        Unreviewed;       855 AA.
AC   A0A268TAF7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574};
GN   ORFNames=BKH45_06215 {ECO:0000313|EMBL:PAF41683.1};
OS   Helicobacter sp. 11S03491-1.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1476196 {ECO:0000313|EMBL:PAF41683.1, ECO:0000313|Proteomes:UP000216568};
RN   [1] {ECO:0000313|EMBL:PAF41683.1, ECO:0000313|Proteomes:UP000216568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11S03491-1 {ECO:0000313|EMBL:PAF41683.1,
RC   ECO:0000313|Proteomes:UP000216568};
RX   PubMed=28827684; DOI=10.1038/s41598-017-09091-7;
RA   Gilbert M.J., Duim B., Timmerman A.J., Zomer A.L., Wagenaar J.A.;
RT   "Whole genome-based phylogeny of reptile-associated Helicobacter indicates
RT   independent niche adaptation followed by diversification in a
RT   poikilothermic host.";
RL   Sci. Rep. 7:8387-8387(2017).
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}.
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:PAF41683.1}.
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DR   EMBL; MLAO01000008; PAF41683.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A268TAF7; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000216568; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216568};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          4..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          411..491
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   855 AA;  96287 MW;  18AA1AF154095250 CRC64;
     MNIFEKMTHQ LKETLDQAVS LALHGKNQEV DTIHLIWAML SNTQSILNQA LHKMNIDKIA
     IELEVKSLAD KLPKSSNITK ENITISKNLQ DNLNQAEGLA TKNGDKYIAL DTFIIANIKT
     EIFTQVFRKY LDLTELKKTL EVIRGGTKIQ NENDDSNLES LEKFGIDLTK KALENTLDPV
     IGRDEEISRM MQILIRKTKN NPILLGEPGV GKTAAVEGLA QRIIKKEVPI SLQNKRVIAL
     DMSALVAGAK YRGEFEERLK KVIEEVKKAG NIILFIDEIH TIVGAGASEG SMDAANILKP
     ALARGELHTI GATTLKEYRK YFEKDAALTR RFQPINLNEP TVNEALQILR GIKEKLEAHH
     NVNITDSALV AAAKLSNRYI TDRFLPDKAI DLIDEGAAEL KMQIESEPTE LSRIKRQIQT
     LEVEKQALNM EKKDTNKTRL EEIDKELSNS NEERNRLEAQ FENEKNVFKE IAQTKSNIDS
     LKRESELAKR EGNYNKAAEI DYSKIPDQEI KEKGLNEKWD KMQASGTLLK NAVTEESIAN
     IISRWTQIPV KKMLQSEKDR ILGVEDELRK SVVGQDKALK AISRVIKRNK AGLSEANRPI
     GSFLFLGPTG VGKTQSAKSL AQFLFDTDKN LIRIDMSEYM EKHAASRLVG APPGYVGYEE
     GGQLTEAVRR KPYSVVLFDE IEKAHPDVFN ILLQVLDDGR LTDNKGVTVD FRNTIIILTS
     NIASDKIIEI NDEKEKAVNE ALKKYFKPEF LNRLDDIIIF NPLDIEGIVK IVDIMFEGIA
     KKVIEKNISL QLTPQAKEFI AKAGFDPVYG ARPLKRALYE EVEDRLAELI LEGKVAEGNK
     VLFDLKDNEI FPQIS
//
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