ID D6ZJF9_MOBCV Unreviewed; 918 AA.
AC D6ZJF9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Putative ATP-dependent chaperone protein ClpB {ECO:0000313|EMBL:ADI66858.1};
GN OrderedLocusNames=HMPREF0573_10539 {ECO:0000313|EMBL:ADI66858.1};
OS Mobiluncus curtisii (strain ATCC 43063 / DSM 2711 / V125) (Falcivibrio
OS vaginalis).
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Mobiluncus.
OX NCBI_TaxID=548479 {ECO:0000313|EMBL:ADI66858.1, ECO:0000313|Proteomes:UP000006742};
RN [1] {ECO:0000313|Proteomes:UP000006742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43063 / DSM 2711 / V125
RC {ECO:0000313|Proteomes:UP000006742};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP001992; ADI66858.1; -; Genomic_DNA.
DR AlphaFoldDB; D6ZJF9; -.
DR STRING; 548479.HMPREF0573_10539; -.
DR KEGG; mcu:HMPREF0573_10539; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_11; -.
DR Proteomes; UP000006742; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 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 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|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000006742};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 4..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 520..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 254..281
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 414..498
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 520..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 99829 MW; B810D97CC40F7EE6 CRC64;
MISMDQKFTT KSQEALATAL RTAGAAGNAM LEPIHLLSAL LEDREGIAFE VLSSVADADA
IGREVRRELA SLPGATGESV AEPQPSQAML NVISAAGAKA QERGDDYVST EHLLLGLAEN
EGRVGKILRD AGANDKKLRQ AIKKIRGDAK VTSPNPEATF KALEKYGDDL TQRAMDGNLD
PVIGRDSEIR RVIQVLSRRT KNNPVLIGEP GVGKTAVVEG LAQRIVAGDV PDSLKHKHLI
ALDLAAMVAG AQYRGQFEER LKAVLEEIKN AEGEVVTFID ELHTVVGAGA SGGSMDASNM
LKPMLARGEL RLVGATTLDE YREHIEKDPA LERRFQTVFV GEPSVEDTVA ILRGIAPKYE
AHHKVTIADG ALVAAAQLSN RYISGRQLPD KAIDLIDEAA SRLRMELDSS PEEIDSLRRE
VERVNMELSY LNASDPNRED PATEGRVAQL QASLDEKQAQ LDRLNLRWEA EKAGHNRVGE
LRVKLDELNT ALEQAMREGR WEDAGRLQNG EIPAIQAQIT AAEGESSNQS SAAGHAPTDS
AISGTNSTKP GHPDAGDSQD GPMIAEKVDA AEIAEVVASW TGIPVGKLLR GESEKLLHME
EYLGQRLIGQ KDAVRAVSNA VRRARAGVSD PNRPTGSFLF LGPTGVGKTE LAKALADFLF
DDEKALTRID MSEYGEKHSV ARLIGAPPGY VGYEEGGQLT EAVRRRPYGV VLLDEVEKAH
PDVYDILLQV LDDGRLTDGQ GRTVDFRNVI LVLTSNLGSQ FLIDREADPA EAHRQVLDLV
RAAFKPEFLN RLDETIMFEA LSTEDLEQIV DIQIHQLTTR LAESQLTLEV TESARSWLAV
TGYDPTYGAR PLRRLIQREI GDQLAEKLLA GDITPGSTVV VDMPNFSPTD LIKSGDLSEL
TGPMSDQYRL ELRVKNAQ
//
