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Database: UniProt
Entry: A0A087EB59_9BIFI
LinkDB: A0A087EB59_9BIFI
Original site: A0A087EB59_9BIFI 
ID   A0A087EB59_9BIFI        Unreviewed;       863 AA.
AC   A0A087EB59;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding protein {ECO:0000313|EMBL:KFJ05010.1};
GN   ORFNames=BISU_1538 {ECO:0000313|EMBL:KFJ05010.1};
OS   Bifidobacterium subtile.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=77635 {ECO:0000313|EMBL:KFJ05010.1, ECO:0000313|Proteomes:UP000029055};
RN   [1] {ECO:0000313|EMBL:KFJ05010.1, ECO:0000313|Proteomes:UP000029055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 11597 {ECO:0000313|EMBL:KFJ05010.1,
RC   ECO:0000313|Proteomes:UP000029055};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675}.
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:KFJ05010.1}.
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DR   EMBL; JGZR01000002; KFJ05010.1; -; Genomic_DNA.
DR   RefSeq; WP_024463742.1; NZ_JGZR01000002.1.
DR   AlphaFoldDB; A0A087EB59; -.
DR   STRING; 77635.BISU_1538; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000029055; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
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; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001943; UVR_dom.
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; PS00871; CLPAB_2; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:KFJ05010.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:KFJ05010.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:KFJ05010.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029055};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          429..464
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          145..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          820..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  95076 MW;  E68E7ED962957808 CRC64;
     MFERFTDRAR RVIVLAQEEA RALQHNYIGT EHLLLGLIRE GEGVAAKALA AKGVNLEDTR
     KQVEEMIGKG NAAPNGHIPF TPHAKQVLEL SLREALQLGH SYIGTEHILL GLIREGEGVG
     TQVLIKMDVD LGELRSSTID MIRGNSASSD ASGKGDLANA GGVQEKGRQT GSAILDQFGR
     NLTAEAAEGK LDPVIGRSNE IERVMVVLSR RTKNNPVLIG EPGVGKTAVV EGLAQKISAG
     DVPETLKDKQ VYSLDLGSMV AGSRYRGDFE ERLKKVLKEI KTRGDIVLFI DEIHTIVGAG
     SADGALGASD MLKPLLARGE LQTIGATTTD EYRKYIEKDA ALERRFQPIQ VHEPTIAETI
     EILKGLRERY ENHHHVTITD GALQSAAELS SRYIQDRNLP DKAIDLIDEA GARLRIKRLT
     APPELKELDS RIARISEQKD QAIKDQDFEK AAELRDSQEK LEDQRKEKEA SWREGGSDVK
     MVVDEDVIAE VISNSTGIPV FKLTQAESKK LLGMESELHK RIIGQDEAVS ALSRSIRRTR
     VGLKDPKRPA GSFIFAGPTG VGKTELAKTL AQFLFDDEDA LIRVDMSEFS EKYAASRLFG
     APPGYVGYEE GGELTEKVRR KPFSVVLFDE IEKAHPDIFN TLLQVLDDGH LTDGQGRKVD
     FKNTIIILTT NLGTRDIAKA ANTGFNLGSN AETSYQRMKD QVTSELKQQF RPEFLNRLDD
     IIVFQQLTEP QVRQIVDLDI SQLNDRLFER HMSLELTDNA KDLLAQKGFD PLLGARPLRR
     VIQRDIEDAI SEQILMGKLE DGQRVLVDSE GEGILGEFTF KGEDFDDPQP QGELVGASVG
     SGDAPVAADV PNAEDHAEDD AEE
//
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