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Database: UniProt
Entry: A0A087BDB5_9BIFI
LinkDB: A0A087BDB5_9BIFI
Original site: A0A087BDB5_9BIFI 
ID   A0A087BDB5_9BIFI        Unreviewed;       863 AA.
AC   A0A087BDB5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=ATPase AAA {ECO:0000313|EMBL:KFI69015.1};
GN   ORFNames=BMERY_0505 {ECO:0000313|EMBL:KFI69015.1};
OS   Bifidobacterium merycicum.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=78345 {ECO:0000313|EMBL:KFI69015.1, ECO:0000313|Proteomes:UP000029060};
RN   [1] {ECO:0000313|EMBL:KFI69015.1, ECO:0000313|Proteomes:UP000029060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 11341 {ECO:0000313|EMBL:KFI69015.1,
RC   ECO:0000313|Proteomes:UP000029060};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KFI69015.1}.
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DR   EMBL; JGZC01000010; KFI69015.1; -; Genomic_DNA.
DR   RefSeq; WP_051915254.1; NZ_JGZC01000010.1.
DR   AlphaFoldDB; A0A087BDB5; -.
DR   STRING; 78345.BMERY_0505; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000029060; Unassembled WGS sequence.
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; -; 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:SF193; CHAPERONE PROTEIN CLPB; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029060};
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          427..462
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          816..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          423..469
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   863 AA;  94017 MW;  470A41AE0EBF0789 CRC64;
     MFERFTDRAR RVIVLAQEEA RALQHNYIGT EHLLLGLIRE GEGVAAKALA SKGVELDATR
     KQVEEMIGKG NASSNGHIPF TSHAKQVLEL SLREALQLGH SYIGTEHILL GLIREGEGVG
     TQVLIKMDVN LGELRSTTID MIRGNAAGGD DKGELANAGG VADKNSRTSS AILEQFGRNL
     TAEAAAGKLD PVIGRTQEIE RVMVVLSRRT KNNPVLIGEP GVGKTAVVEG LAEKINAGDV
     PETLKDKQVY SLDLGSMVAG SRYRGDFEER LKKVLKEIKS RGDIVLFIDE IHTIVGAGSA
     DGALGASDML KPMLARGELQ TIGATTTDEY RKYIEKDAAL ERRFQPIQVH EPTIAETIEI
     LKGLRERYEN HHRVTITDSA IQAAAELSSR YIQDRRLPDK AIDLIDEAGA RLRIKRLTTP
     PELKELEAKV AKVSAEKEQA VKDQDFEKAA AMRDDLESLQ NELKDKETAW HEGGSDVIAE
     VVSSTTGIPV VKLTQAESKK LLNMEAELHK RIIGQDEAVS ALSRSIRRTR VGLKDPKRPS
     GSFIFAGPTG VGKTELAKTL AEFLFDDEDA LIRVDMSEFS EKYAASRLFG APPGYVGYEE
     GGELTEKVRR KPFSVVLFDE IEKAHPDIFN TLLQVLDDGH LTDGQGRKVD FKNTIIILTT
     NLGARDIAKA ANTGFSLGTN SESSYQRMKE QVSSELKQQF RPEFLNRLDD IIVFKQLTEP
     EVRQIVDLDV KQLNDRLFDR HMELDLTDKA KDLLAQKGFD PLLGARPLRR VIQRDIEDAI
     SEKILMGELT DGERVKVDAE GEGVLGDFIF TGEAFDAGEG DSAGAESGSA GAGAESGSAG
     AGSADSTAPE TPAAPDAPGS LSE
//
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