ID A0A553ZQI6_9ACTN Unreviewed; 865 AA.
AC A0A553ZQI6;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:TSB43734.1};
GN ORFNames=FNZ23_02595 {ECO:0000313|EMBL:TSB43734.1};
OS Streptomyces benahoarensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2595054 {ECO:0000313|EMBL:TSB43734.1, ECO:0000313|Proteomes:UP000320888};
RN [1] {ECO:0000313|EMBL:TSB43734.1, ECO:0000313|Proteomes:UP000320888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZ03-48 {ECO:0000313|EMBL:TSB43734.1,
RC ECO:0000313|Proteomes:UP000320888};
RA Gonzalez-Pimentel J.L.;
RT "Draft genome for Streptomyces benahoarensis MZ03-48.";
RL Submitted (JUL-2019) 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, ECO:0000256|RuleBase:RU004432}.
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:TSB43734.1}.
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DR EMBL; VKLS01000013; TSB43734.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A553ZQI6; -.
DR Proteomes; UP000320888; 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; 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 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; 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, ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:TSB43734.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TSB43734.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000320888};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 39..178
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 170..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 447..486
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 174..188
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 93091 MW; 4E8A1051F514EEF0 CRC64;
MSDGFMGPEG FEPDPFGDFL GRVFGRSGGS SRAPMQADIA RLMSAGARDL VTSAATYAAD
HGSTELSTEH LLRAALTTEP TRSLVRQSGA DPDALAANID RSAGTGPQQS RVAVTPAVKR
ALLGAHDMAL GGGASYIGPE HVLEALAANP DSAAGRILNV FRIDAQHAER NAAPGHPPVP
PEPGAPPRHE TPTLDKYSRD LTEVARAGRI DPVIGREAEI EQTIEVLSRR GKNNPVLVGD
AGVGKTAIVE GLAQRMADGE VPETLAGRRV VSLDMTGVVA GTRYRGDFEE RLNAIIEEVR
AHSDSLIVFI DELHTVVGAG GGSDGGGMDA SNILKPALAR GELHVIGATT LEEYRRYIEK
DAALARRFQP LLVPEPDVAD AVEILRGLQD RYEAHHQVRY TDEALRAAVE LSDRYLADRF
LPDKAIDLID QAGARVRLRS GTKAAGVRGL EREVEQLTRD KDQTVAAEQY ERATELRDRI
AELTERIGAG TGEVPGDGRI VEVTAADVAE IISRHTGIPV SNLTEEERER LLGLEERLHA
RVIGQDDAVA AVAEAVLRSR AGLADPQRPI GSFLFLGPTG VGKTELARAL AEVLFGSEDR
MVRLDMSEYQ ERHTVSRLVG APPGYVGHED AGQLTEAVRR HPYALVLLDE VEKAHPDVFN
MLLQVLDDGH LTDAQGRTVD FKNTVIVMTS NLGSEALSGG RGTLGFGPSG GDGDDGARER
AMAALRTHFR PEFLNRLDEI IVFRQLSDAQ LREITALLLD ATSRRMRAQD MTIEFSPEAV
DWLTRRGHRP EYGARPLRRT IQREIDNALS RLVLDGALSL GDRIRVEIED DRPAFRTTPG
GEPAPGAEPP GGATADGSPE EPSGG
//