ID A0A2P1PNL1_9GAMM Unreviewed; 858 AA.
AC A0A2P1PNL1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=C7S18_04130 {ECO:0000313|EMBL:AVP96431.1};
OS Ahniella affigens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Ahniella.
OX NCBI_TaxID=2021234 {ECO:0000313|EMBL:AVP96431.1, ECO:0000313|Proteomes:UP000241074};
RN [1] {ECO:0000313|EMBL:AVP96431.1, ECO:0000313|Proteomes:UP000241074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D13 {ECO:0000313|EMBL:AVP96431.1,
RC ECO:0000313|Proteomes:UP000241074};
RA Ko Y., Kim J.-H.;
RT "Ahniella affigens gen. nov., sp. nov., a gammaproteobacterium isolated
RT from sandy soil near a stream.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AVP96431.1, ECO:0000313|Proteomes:UP000241074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D13 {ECO:0000313|EMBL:AVP96431.1,
RC ECO:0000313|Proteomes:UP000241074};
RA Keele B.F.;
RL Submitted (MAR-2018) 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. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP027860; AVP96431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P1PNL1; -.
DR KEGG; xba:C7S18_04130; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000241074; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
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; IPR017730; Chaperonin_ClpB.
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 InterPro; IPR002078; Sigma_54_int.
DR NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 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.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 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|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000241074};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 570..803
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT COILED 405..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 858 AA; 96462 MW; 29060A2CC5DA3736 CRC64;
MRMDKLTSHF QQALQEAQSL AVGRDHNMLE PLHLLTTLIE QQGGSIRPLL TKLSVNVPGV
RAKLGQMLDA LPKIKGQEGN LNVSNDLNRL LNITDKLAQQ RNDQFIASEL FLLALVQDRH
ELGDLLRKHG VKPEALSEAI DEVRGGQSVQ DQSAEEHRQA LSKYTIDYTE RAEQGKLDPV
IGRDEEIRRV VQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIIKGEVPE GLRDKRLLSL
DMGALIAGAK YRGEFEERLK AVLNDLAKQE GRVVLFIDEL HTMVGAGKAE GAMDAGNMLK
PALARGELHC VGATTLDEYR KYIEKDAALE RRFQKVFVGE PSVEDTIAIL RGLKERYAVH
HGVEITDPAI VAAATLSNRY IADRQLPDKA IDLMDEAASR IRMEIDSKPE ELDRLERRLI
QLKIQREALK KEKDNESKQR LADLETDISK LEREFSDLEE IWKSEKAAVQ GTTKIKEEIE
RAKTEMDHAL RNQDFAKLSE IQYGRLPQLE KQLEAAHATE TQGFKLLQQK VTADEIAEVV
SRWTGIPVSK MLEGERDKLL RMEDELHKRV VGQDEAVRAV ADAIRRSRAG LSDPNRPNGS
FLFLGPTGVG KTELCKALAD FMFDSTDAMV RIDMSEFMEK HSVSRLIGAP PGYVGYDEGG
YLTEAVRRRP YSVILLDEVE KAHPDVFNVL LQVLDDGRLT DGQGRTVDFR NTVVVMTSNL
GSQMIQEYAA RNDYQGMRTA VMEVVQSHFR PEFINRLDEL VVFHPLGREH IRNIARIQTQ
HLAKRLADRQ IKISISDSAL DLLGNVGFDP VYGARPLKRA IQTQLENPLA SRILAGEYSA
QDTIIVDVFN GQMQFRKQ
//