ID D3UI70_HELM1 Unreviewed; 855 AA.
AC D3UI70;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574};
GN Name=clpB {ECO:0000313|EMBL:CBG40193.1};
GN OrderedLocusNames=HMU09360 {ECO:0000313|EMBL:CBG40193.1};
OS Helicobacter mustelae (strain ATCC 43772 / LMG 18044 / NCTC 12198 / 12198)
OS (Campylobacter mustelae).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=679897 {ECO:0000313|EMBL:CBG40193.1, ECO:0000313|Proteomes:UP000001522};
RN [1] {ECO:0000313|EMBL:CBG40193.1, ECO:0000313|Proteomes:UP000001522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43772 / LMG 18044 / NCTC 12198 / 12198
RC {ECO:0000313|Proteomes:UP000001522};
RX PubMed=20219135; DOI=10.1186/1471-2164-11-164;
RA O'Toole P.W., Snelling W.J., Canchaya C., Forde B.M., Hardie K.R.,
RA Josenhans C., Graham R.L.J., McMullan G., Parkhill J., Belda E.,
RA Bentley S.D.;
RT "Comparative genomics and proteomics of Helicobacter mustelae, an
RT ulcerogenic and carcinogenic gastric pathogen.";
RL BMC Genomics 11:164-164(2010).
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; FN555004; CBG40193.1; -; Genomic_DNA.
DR RefSeq; WP_013023266.1; NC_013949.1.
DR AlphaFoldDB; D3UI70; -.
DR STRING; 679897.HMU09360; -.
DR KEGG; hms:HMU09360; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_7; -.
DR Proteomes; UP000001522; 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; 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 Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:CBG40193.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CBG40193.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001522};
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..523
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 855 AA; 96006 MW; E2D416D851FA95DB CRC64;
MNIFEKLTNP LKENLDSAAA LALHQKNQEI DLIHIAWALL NTPQSLLNQA LDKMQQNSRE
IELIVRSNAE KLPKVSHIEK ENLSLSKGLQ KALQEAEGLA IKNGDKFIAI DTLILANLKE
FGEILGGGIE LLELKKTLQS LRAGRKIEDA GGDCMLEALE KFGIDLTKKA QDNLLDPVIG
RDEEITRMMQ ILIRKTKNNP ILLGEPGVGK TAVVEGLAQQ IIKKEVPLSL QNKRIIVLDM
SLLVAGAKYR GEFEERLKNI LEEVKKAGNI ILFIDEIHTI VGAGASEGSM DAANILKPAL
ARGELHTIGA TTLKEYRKYF EKDAALTRRF QPIFLNEPSI SEALQILRGL KEKLETHHNV
SITDSALVAA VKLSHRYITD RFLPDKAIDL IDEGAAELKM QIESEPSALR NIKRVIQRLE
VEKEALHMEN KPTNANRLEE LEKELANQVE KKNSLQMQFD NEKSVFKEIA QMKNTIDALK
RESEIAKRNG DYNKAAEIDY AKIPEAQNQE KSLQDRWEEM QKNGTLLQNA LTEESIAEIV
SRWTQIPVKR MLQEEREKIL NIELELRKSV VGQDEALHAI ARAIKRNKAG LSSSNHPIGS
FMFLGPTGVG KTQSAKSLAE FLFLSQKNLI RIDMSEYMEK HAASRLVGAP PGYVGYEEGG
QLTEAVRRKP YSVVLFDEIE KAHPDVFHIL LQVLDDGRLT DNKGVVVDFR NTIIILTSNI
ASDKILELKD REEKKRAVES SLKQYFKPEF LNRLDDIVIF NPLDLGGIVE IVDIMFDSIA
KKLIERGIVV ELESAAKEWI AQVGFDPIYG ARPLKRALYE QIEDALAELI LQDKIKEGSK
VVFAVKNDAI EAQIS
//
