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Database: UniProt
Entry: A0A4Q8AG87_9MICC
LinkDB: A0A4Q8AG87_9MICC
Original site: A0A4Q8AG87_9MICC 
ID   A0A4Q8AG87_9MICC        Unreviewed;       853 AA.
AC   A0A4Q8AG87;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:RZU63308.1};
GN   ORFNames=EV380_2924 {ECO:0000313|EMBL:RZU63308.1};
OS   Zhihengliuella halotolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Zhihengliuella.
OX   NCBI_TaxID=370736 {ECO:0000313|EMBL:RZU63308.1, ECO:0000313|Proteomes:UP000292685};
RN   [1] {ECO:0000313|EMBL:RZU63308.1, ECO:0000313|Proteomes:UP000292685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17364 {ECO:0000313|EMBL:RZU63308.1,
RC   ECO:0000313|Proteomes:UP000292685};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (FEB-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:RZU63308.1}.
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DR   EMBL; SHLA01000001; RZU63308.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q8AG87; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000292685; 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   GO; GO:0006355; P:regulation of DNA-templated transcription; 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; 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; IPR002078; Sigma_54_int.
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; PS50045; SIGMA54_INTERACT_4; 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:RZU63308.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RZU63308.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000292685};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          429..464
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   DOMAIN          522..787
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000259|PROSITE:PS50045"
FT   REGION          147..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          425..471
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   853 AA;  93651 MW;  9D599C6162837923 CRC64;
     MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKALE SLSISLGAVR
     EQVQEIIGQG QQAPSGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGVA
     AQVLVKLGAD LNRVRQQVIQ LLSGYQGGSG GKETAGAGVS SGGQQEGTPA GSAVLDQFGR
     NLTAAAREGK LDPVIGREHE MERVMQVLSR RTKNNPVLIG EPGVGKTAVV EGLAQSIVRG
     DVPETIKDKQ LYTLDLGSLV AGSRYRGDFE ERLKKVLKEI RTRGDIILFI DEIHTLVGAG
     AAEGAIDAAS ILKPMLARGE LQTIGATTLD EYRKHIEKDA ALERRFQPIQ VGEPSVEHTT
     QILRGLRDRY EAHHRVSITD DALAAAASLA HRYISDRFLP DKAIDLIDEA GARLRIQRMT
     APPELKEMDE EIANVRREKE AAIDSQDFEG AASLRDKEQK LQDARNEKEK SWKNGDMDSI
     AEVNEELIAE VLANSTGIPV VKLTEEESTR LLNMEDALHK RVIGQNQAIK AISRAIRRTR
     AGLKDPNRPT GSFIFAGPTG VGKTELAKAL AEFLFGEEDA LITLDMSEYQ EKHTVSRLFG
     APPGYVGYEE GGQLTEKVRR RPFSVVLFDE VEKAHSDLFN SLLQILEDGR LTDSQGRVVD
     FKNTVIIMTT NLGTRDISKG VMTGFQSSSD TATGYDRMQA KVQEELRQHF RPEFLNRVDD
     VVVFPQLTEK EIVEIVDLFV NRLEKRMVEK GMHVDLSTAA KALLATRGYD SSMGARPLRR
     TIQRDIEDQL SEKILFGEIV SGQTVKVDVE GEGDSAKFTF TGIDTPAEIE GEPVPAAIES
     AAAADPAEAD QAS
//
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