ID A0A399CU92_9BACT Unreviewed; 862 AA.
AC A0A399CU92;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RIH62728.1};
GN ORFNames=D1164_23430 {ECO:0000313|EMBL:RIH62728.1};
OS Mariniphaga sediminis.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Mariniphaga.
OX NCBI_TaxID=1628158 {ECO:0000313|EMBL:RIH62728.1, ECO:0000313|Proteomes:UP000266441};
RN [1] {ECO:0000313|EMBL:RIH62728.1, ECO:0000313|Proteomes:UP000266441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY21 {ECO:0000313|EMBL:RIH62728.1,
RC ECO:0000313|Proteomes:UP000266441};
RX PubMed=26012581; DOI=10.1099/ijs.0.000354;
RA Wang F.Q., Shen Q.Y., Chen G.J., Du Z.J.;
RT "Mariniphaga sediminis sp. nov., isolated from coastal sediment.";
RL Int. J. Syst. Evol. Microbiol. 65:2908-2912(2015).
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 -!- 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:RIH62728.1}.
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DR EMBL; QWET01000047; RIH62728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399CU92; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000266441; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000266441};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 396..521
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 862 AA; 97634 MW; 181AF38A6D581899 CRC64;
MNLNNFTIKA QEAIQHAFQI AAGNNQQSIE TGHVLKGLSH SAENVLDFLL KKLGVNTVIF
QQAADKIIES YPRVSGGEPY ISTTTNRVLQ KALALAQEMG DQYVSVEHIL LALLDANDSV
SRLMKDNGVT KKDLQKAIEE LRKGSKVDSQ TAEDRFNSLN RFALNLNERA RSGKLDPVIG
RDEEIRRILQ ILSRRTKNNP ILIGEPGTGK TAIAEGLAHR IVRGDVPENL KTKQVFSLDM
GALIAGAKYK GEFEERLKAV VHEVVHSNEE VILFIDEIHT LVGAGKSDGA MDAANILKPA
LARGELRAIG ATTFNEYQKY FEKDKALERR FQVVQVNEPD TLSAISILRG IKERYESHHK
VRIKDDAIIA SVELSQRYIS DRFLPDKAID LMDEAAAKLR LEMDSVPEEL DEIERRIKQL
EIEREAIKRE KDDKKLATLS EEISNLKEEQ SQLRAKWQSE KQIIDSIQQK KSEIEDYRVE
AEEAERQGHY DRVAELRYGK IKEAENVIGD LQKELQKMKK GESLIKEEVD AEDIAEVVAR
WTGIPVAKML QSERVKLLHM EEELHKRVVG QDEAIAAVSD AVRRSRAGLQ DEKRPIGSFI
FLGSTGVGKT ELAKALAEYL FDDENMITRI DMSEYQEKFS VTRLIGSPPG YVGYDEGGQL
TESVRHKPYS VVLFDEIEKA HPDVFNVLLQ VLDDGRLTDN KGRTVNFKNT IIIMTSNLGS
HLIQESFENI KTDNEVAVVE EMRIRLLELL RKTIRPEFLN RIDETIVFTP LSREDINHIV
KLQFNQVVKR LSGTDVKMSL TDAAVDWLAA ISYDPHFGAR PVKRILQKYV LNELSRKILA
AEVDKRNPIV VDVEDERLIF RN
//
