ID A0A0F5F252_AVIPA Unreviewed; 857 AA.
AC A0A0F5F252;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:SUV40373.1};
GN ORFNames=NCTC10926_02411 {ECO:0000313|EMBL:SUV40373.1};
OS Avibacterium paragallinarum (Haemophilus gallinarum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Avibacterium.
OX NCBI_TaxID=728 {ECO:0000313|EMBL:SUV40373.1, ECO:0000313|Proteomes:UP000254620};
RN [1] {ECO:0000313|EMBL:SUV40373.1, ECO:0000313|Proteomes:UP000254620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10926 {ECO:0000313|EMBL:SUV40373.1,
RC ECO:0000313|Proteomes:UP000254620};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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}.
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DR EMBL; UFSW01000002; SUV40373.1; -; Genomic_DNA.
DR RefSeq; WP_046097736.1; NZ_VXDA01000048.1.
DR AlphaFoldDB; A0A0F5F252; -.
DR STRING; 728.VY92_03165; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000254620; Unassembled WGS sequence.
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: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 NCBIfam; TIGR03346; chaperone_ClpB; 1.
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|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Stress response {ECO:0000256|RuleBase:RU362034,
KW ECO:0000313|EMBL:SUV40373.1}.
FT COILED 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 857 AA; 96295 MW; DBE3FB22C00A62C5 CRC64;
MNIEKFTTRF QQALSEAQSL ALGKDNQFIE PVHLMTALLN QEGGSIAPIL TASGVNVALF
RNELNAELNR LPQVSGNGGD VQISRNLVNL LNLCDKLAQQ KQDKYISSEL FLLAALEEKG
NLSEILRKCG AKKEHLQQAI NQIRGGQSVN DQNAEESRQA LEKYTIDLTA RAESGKLDPV
IGRDEEIRRT IQVLQRRSKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKNKRVLSL
DMGALIAGAK YRGEFEERLK AVLNEIAKEE GRIILFIDEI HTMVGAGKTD GAMDAGNLLK
PSLARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVDE PSVEDTIAIL RGLKERYEIH
HHVQITDPAI VAAATLSHRY ISDRQLPDKA IDLIDEAASS IRMEIDSKPE PLDRLDRRII
QLKLEQQALQ KEDDDASRKR LEMLEKELVE KEREYAELEE VWKSEKAALS GTQHIKAELE
NAKTQMEQAR RVGDLNKMSE LQYGRIPELE KQLAQAESAE NKEMHLLRYR VTDEEIAEVL
SRATGIPVSK MMEGEKEKLL RMEKELHKRV VGQNEAVEAV ANAIRRSRAG LSDPNRPIGS
FLFLGPTGVG KTELCKTLAK FLFDDETAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG
YLTEAVRRRP YSVVLLDEVE KAHADVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
GSDLIQTNRD LDYSAMKELV MSVVSQHFRP EFINRIDETV VFHPLDKENI RTIAKIQLQR
LEKRMETHGY HLEFTDAALD FIGEIGYDPI YGARPLKRAI QQEVENPLAQ KILSGELLPG
KPITIDYVDG NIITRQS
//
