ID S2Z248_9CORY Unreviewed; 852 AA.
AC S2Z248;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=HMPREF1219_01530 {ECO:0000313|EMBL:EPD68350.1};
OS Corynebacterium pyruviciproducens ATCC BAA-1742.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1125779 {ECO:0000313|EMBL:EPD68350.1, ECO:0000313|Proteomes:UP000014408};
RN [1] {ECO:0000313|EMBL:EPD68350.1, ECO:0000313|Proteomes:UP000014408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1742 {ECO:0000313|EMBL:EPD68350.1,
RC ECO:0000313|Proteomes:UP000014408};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Tong J., Walker B., Young S.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Corynebacterium pyruviciproducens 1773O (ATCC BAA-
RT 1742).";
RL Submitted (MAY-2013) 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|ARBA:ARBA00004496,
CC 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:EPD68350.1}.
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DR EMBL; ATBY01000015; EPD68350.1; -; Genomic_DNA.
DR RefSeq; WP_016458276.1; NZ_KE150447.1.
DR AlphaFoldDB; S2Z248; -.
DR STRING; 1125779.HMPREF1219_01530; -.
DR PATRIC; fig|1125779.3.peg.1491; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_11; -.
DR Proteomes; UP000014408; 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:UP000014408};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 253..280
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 414..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 852 AA; 93040 MW; 43D05C656190CB75 CRC64;
MSDFTPTTKT GEALQTALQL ASGKGNPDIR PAHILVAIVE QQDGVAAPVL KAAGVAPQVI
ATEARKLVDG YPSASGSNMA NPNFNRSALN AFNAAQELAG ELGDEYVSTE VLLAGIARGD
SDAAKMLARH GATYENIKAA FEQVRGGHKV TNADPENQFQ ALEKYSTDLT ERARQGKIDP
VIGRDQEIRR VMQVLSRRTK NNPVLIGEPG VGKTAIVEGL ARRIVAGDVP ESLKNKKLIS
LDLGSMVAGA KYRGEFEERL KAVLEEIKNA EGEIITFIDE LHTIVGAGAT GDSAMDAGNM
IKPLLARGEL RLVGATTLDE YRKYIEKDAA LERRFQQVYV GEPSVEDGIG ILRGLKERYE
VHHGVRIQDS ALVAAVTLSD RYITNRYLPD KAIDLIDEAA SRLRMEIDSS PQEIDEAERI
VRRLEVEELA LQKETDAASK ERLEKLRREL ADEKEKLSEL RARWANEKEA ISHVQKAKEE
LDRLRTESEE AEREGDLAKL SEIRYGKIPA AEKALAEAEQ VVNSEQDTML TEEVTPDTIA
EVVSAWTGIP AGKMLQGETE KLLHMEAELG KRVVGQTDAV TAVSDAVRRA RAGVADPNRP
TGSFLFLGPT GVGKTELAKA LAEFLFDDER AMVRIDMSEY GEKHSVARLV GAPPGYVGYD
QGGQLTEAVR RRPYTVVLFD EVEKAHPDVF DILLQVLDDG RLTDGQGRTV DFRNTLLILT
SNLGAGGTKD EMMAAVKRTF KPEFVNRLDD VVVFDALSPE QLTGIVDIQV GQLAERLAAR
RLTLQVSDAA KSWLASRGYD PAYGARPLRR LIQQAIGDTL ARKLLAGDVR DGDTVHVDVA
ADGESLDIAP VR
//