ID D7C6C8_STRBB Unreviewed; 846 AA.
AC D7C6C8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Clp protease ATP binding subunit {ECO:0000313|EMBL:ADI04116.1};
GN OrderedLocusNames=SBI_00995 {ECO:0000313|EMBL:ADI04116.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI04116.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI04116.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI04116.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
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; CP002047; ADI04116.1; -; Genomic_DNA.
DR RefSeq; WP_014173595.1; NC_016582.1.
DR AlphaFoldDB; D7C6C8; -.
DR STRING; 749414.SBI_00995; -.
DR KEGG; sbh:SBI_00995; -.
DR PATRIC; fig|749414.3.peg.1017; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_11; -.
DR Proteomes; UP000000377; Chromosome.
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; IPR018368; ClpA/B_CS1.
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 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.
DR PROSITE; PS50151; UVR; 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};
KW Hydrolase {ECO:0000313|EMBL:ADI04116.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ADI04116.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 40..179
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 451..486
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 165..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 846 AA; 92870 MW; 92DF8E43AAFD9387 CRC64;
MNSGYEGSEE FGPDPLGDFL ARFLGVGPAG QRPGSRHVDF GRLMSEPARQ LVSSAASYAA
DRGSTDLDTE HLLRAALTAE PTRTMVVRAG ADPEALVAEI DRQTGEGPPR GSVAVTPAVK
RALLDAHEIA RSSGSSYIGP EHVLIALAAN HDSTAGQLLH AARFEPRPGP PGGLAAAPGA
AEPRPGPNRR ETPNLDKFGR DLTEMARDGR IDPVIGRDEE IEQTIEVLAR RGKNNPVLIG
EAGVGKTAVV EGLAQRIAEA DVPDILLARR VLQLDFAGVV AGTRYRGDFE ERLTGIIDEI
RAHSEELIVF IDELHTVVGT GGSEGGPMDA SNILKPALAR GELHVIGAST LQEYRRHIEK
DAALARRFQP IMVPEPTPSD ALEILRGLRD RYEAHHQVRY TDQALLAAVE LSDRYLTDRF
LPDKAIDLMD QAGARVRLRS STRGTDIRAL EREVEQLTRD KDQAVAAEQY ERATSLRDRI
GDLSRRIEEG SGKQHPAGRV AEVTVEDIAD IVSRQTGIPV SSLTQEERDR LLSLEEHLHK
RVIGQEEAVS AVADSVLRSR AGLADPGRPI GSFLFLGPTG VGKTELARAL AEALFGSEDR
MVRLDMSEYQ EKHTVSRLIG APPGYVGHEE AGQLTEAVRR QPYSLLLLDE VEKGHADVFN
ILLQVLDDGR LTDAQGRTID FKNTVIVMTS NLGSEEISGR GAVMGFGGGA EADEDARRER
VLRPLREHFR PEFLNRIDEI VIFRRLADEQ LRQITDVLLE ETRRRLRAQD VPIDFTPAAV
DWLAHHGYQP EYGARPLRRT IQREVDNPLS RMLLNGKLQP HSHVEVDVED GKLTFRKEQN
PTTTLG
//
