ID A0A220VBX4_9GAMM Unreviewed; 888 AA.
AC A0A220VBX4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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:ASK77839.1};
GN ORFNames=CF386_01550 {ECO:0000313|EMBL:ASK77839.1};
OS Paraphotobacterium marinum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Paraphotobacterium.
OX NCBI_TaxID=1755811 {ECO:0000313|EMBL:ASK77839.1, ECO:0000313|Proteomes:UP000242175};
RN [1] {ECO:0000313|EMBL:ASK77839.1, ECO:0000313|Proteomes:UP000242175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSCS20N07D {ECO:0000313|EMBL:ASK77839.1,
RC ECO:0000313|Proteomes:UP000242175};
RX PubMed=27154455; DOI=10.1099/ijsem.0.001142;
RA Huang Z., Dong C., Shao Z.;
RT "Paraphotobacterium marinum gen. nov., sp. nov., a member of the family
RT Vibrionaceae, isolated from surface seawater.";
RL Int. J. Syst. Evol. Microbiol. 66:3050-3056(2016).
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; CP022355; ASK77839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220VBX4; -.
DR KEGG; pmai:CF386_01550; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000242175; Chromosome large.
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 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.
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:UP000242175};
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 COILED 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 888 AA; 99924 MW; A3CB8F06F7DB2CE3 CRC64;
MRLDKFTTKF QEALSESQSL AIGSDNQYVE PVHLLYSLIN QSNSSISPLL QLLKVDVPSF
KEHLSSILNN QPKVSGANVN VQISQQLLTL LNLSDKLSQK RNDKYISSEM FLLALFENSN
QLSDLLTKYN LTKVNVENAI DKIRGGESVE EQNSEESRQA LEKYTIDLTK RAEEGKLDPV
IGRDEEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLSDKKVLSL
DLGALIAGAK FRGEFEERLK AVLKELAKEE GKVILFIDEI HTMVGAGKTD GAMDAGNMLK
PALARGELHC VGATTLDEYR KYIEKDAALE RRFQKVLVEQ PTVEDTIAIL RGLKERYEIH
HHVDITDPAI VAAARLSNRY LTDRQLPDKA IDLIDEAASS IRMQIDSKPE SMDRLERKLI
QMKIEVQALE KESDDASKKR LTSLNKEISK KEKEYSDLDE VWKAEKASLS GTQNIKLELD
KTKNELELAR RSGDLNKMSE LQYGKIPELE KQLNLASQAE NQEMTLLKNR VTEDEIAAIL
SKQTGIPVSK MLEGEKEKLL NMETVLHRSV IGQKEAVDAV SNSIRRNRAG LSDPNRPIGS
FLFLGPTGVG KTELCKGLAN FLFDSKEAMI RLDMSEYMEK HSVSRLVGAP PGYVGYDEGG
YLTEAIRRKP YSVVLLDEVE KAHPDVFNIL LQVLDDGRLT DSQGRTVDFK NTVLIMTSNL
GSDKIQEFFN ERLNNDDVVD SIVDEELDSK GSLKEHLQEN KEQVDYELVK TKVMEVVGAY
FRPEFINRID ESVVFHPLSE DNIKQIARIQ LNQLGERLRD RDYQIVFDEN TVSFVAKAGY
DPIFGARPLK RAIQNYIENP LSKDILSGKL LPKTEIEVSY VDGSLEIK
//