ID V2UE57_9GAMM Unreviewed; 859 AA.
AC V2UE57;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=P255_00929 {ECO:0000313|EMBL:ESK52768.1};
OS Acinetobacter brisouii CIP 110357.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1341683 {ECO:0000313|EMBL:ESK52768.1, ECO:0000313|Proteomes:UP000018418};
RN [1] {ECO:0000313|EMBL:ESK52768.1, ECO:0000313|Proteomes:UP000018418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110357 {ECO:0000313|EMBL:ESK52768.1,
RC ECO:0000313|Proteomes:UP000018418};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter brisouii CIP 110357.";
RL Submitted (OCT-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|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:ESK52768.1}.
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DR EMBL; AYEU01000003; ESK52768.1; -; Genomic_DNA.
DR RefSeq; WP_004903948.1; NZ_KI530762.1.
DR AlphaFoldDB; V2UE57; -.
DR STRING; 396323.VH98_07340; -.
DR PATRIC; fig|1341683.3.peg.922; -.
DR HOGENOM; CLU_005070_4_2_6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000018418; 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:UP000018418};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..143
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 409..458
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 859 AA; 95358 MW; 1F6EEAEEBD24542F CRC64;
MQFEKFTNRL QQTLSDAQSL AMGKDHTAID NIHILAALLK EASNLSLLQQ AGARIPELKQ
KLDQALNDAA TLANPTGEIN LNPDAVKMLN LADRYAQKAG DEFLSTDWVL LALAEVGATK
NILNNTGVTV EGLRKVIESI RGNEKVMSNT HEDQRDSLNK YTIDLTERAA SGKLDPVIGR
DDEIRRTIQV LSRRTKNNPV LIGEPGVGKT AIVEGLAQRI INGEVPESLK DKRVLSLDLG
SLLAGAKYRG EFEERLKAVL NDLAKQEGRV ILFIDELHTL VGAGKTDGAM DAGNMLKPAL
ARGELRCVGA TTLDEYRQYI EKDAALERRF QKVLVDEPSV EDTIAILRGL KERYEVHHGV
KILDSAIIAA AKMSHRYITD RMLPDKAIDL IDEAASRIKM ELDSKPEALD KLERRLIQLK
MQLEAVKKDQ DVGSKAEVAH LEKQIIEVQQ EYNDLEEVWK AEKTLAEGDK KAQVELDKAR
VALEKAIRDG DLAEASRLQY GVIPELQKQL AQDEVVEEAE EPKLLRNKVT DNEIAEVVSA
ATGIPVSKML QGEREKLLHM EEFLHNRVVG QDEAVVAVSN AVRRSRAGLS DPNRPSGSFL
FLGPTGVGKT ELTKALANFL FDSDDAMIRI DMSEFMEKHS VSRLVGAPPG YVGYEEGGVL
TEAVRRKPYS VVLFDEVEKA HPDVFNILLQ VLDDGRLTDS QGRVVDFKNT VIVMTSNLGS
QDVRELGEHA HDDEIRTVVM NAVSQHFRPE FINRIDELVI FHSLKKVQIR GIADIQLSRL
RSRLTEKDMS LTVEDSAFDS LIDAGFDPVY GARPLKRAIQ QQVENSLAQK ILSGEFLPGD
NIVISAENGQ LQFSKMKLS
//
