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
//