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Database: UniProt
Entry: A0A087DIJ7_9BIFI
LinkDB: A0A087DIJ7_9BIFI
Original site: A0A087DIJ7_9BIFI 
ID   A0A087DIJ7_9BIFI        Unreviewed;       880 AA.
AC   A0A087DIJ7;
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=Negative regulator of genetic competence ClpC/MecB {ECO:0000313|EMBL:KFI95347.1};
GN   ORFNames=BSCA_1310 {ECO:0000313|EMBL:KFI95347.1};
OS   Bifidobacterium scardovii.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=158787 {ECO:0000313|EMBL:KFI95347.1, ECO:0000313|Proteomes:UP000029033};
RN   [1] {ECO:0000313|EMBL:KFI95347.1, ECO:0000313|Proteomes:UP000029033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21589 {ECO:0000313|EMBL:KFI95347.1,
RC   ECO:0000313|Proteomes:UP000029033};
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:KFI95347.1}.
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DR   EMBL; JGZO01000003; KFI95347.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087DIJ7; -.
DR   STRING; 158787.BSCA_1310; -.
DR   eggNOG; COG0542; Bacteria.
DR   Proteomes; UP000029033; 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   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};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029033};
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          428..463
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          453..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          819..880
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   880 AA;  96554 MW;  F0D5DAC0C230BFE5 CRC64;
     MFERFTDRAR RVIVLAQEEA RTLQHNYIGT EHLLLGLIRE GEGVAAKALA AKGVTLEDTR
     KQVEEMIGKG NAAPNGHIPF TPHAKQVLEL SLREALQLGH SYIGTEHILL GLIREGEGVG
     TQVLIKMDVD LGELRSATID MIRGNSATTD AGKGDLANAG GVQDKRSQTG SAILDQFGRN
     LTAEAAEGKL DPVIGRSKEI ERVMVVLSRR TKNNPVLIGE PGVGKTAVVE GLAQKINAGD
     VPETLKGKQV YSLDLGSMVA GSRYRGDFEE RLKKVLKEIK TRGDIVLFID EIHTIVGAGS
     ADGALGASDM LKPMLARGEL QTIGATTTDE YRKYIEKDAA LERRFQPIQV HEPTIAETIE
     ILKGLRSRYE NHHKVTITDG ALQSAAELSA RYIQDRNLPD KAIDLIDEAG ARLRIKRLTA
     PPELKELDQK IAKLAGEKDE AIKGQDFEKA AELRDSQEKL EAERKSKEAS WREGGSDVKM
     VVDEDVIAEV ISNTTGIPVF KLTQAESKKL MNMESELHKR IIGQDEAVSA LSRSIRRARV
     GLKDPKRPAG SFIFAGPTGV GKTELAKTLA EFLFDDEDAL IRVDMSEFSE KYAASRLFGA
     PPGYVGYEEG GELTEKVRRK PFSVVLFDEI EKAHPDIFNT LLQVLDDGHL TDGQGRKVDF
     KNTIIILTTN LGTRDIAKAA NTGFNLGSNN ESSYQRMKDQ VSSELKQQFR PEFLNRLDDI
     IVFRQLTEPE VRQIVDLDVK QLNDRLFDRH MSLELTDAAK DLLAQKGFDP LLGARPLRRV
     IQRDIEDAIS EKILMGELED GQKVTVDTEG DNVLDEEFTF KGEDFEQPKP AEGAEGDAAG
     DAAAAGAEDA EAEAPAGDDQ PKFVSASDAA AGDRTETPRQ
//
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