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Database: UniProt
Entry: E3B7D7_9MICO
LinkDB: E3B7D7_9MICO
Original site: E3B7D7_9MICO 
ID   E3B7D7_9MICO            Unreviewed;       874 AA.
AC   E3B7D7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=ATPase family associated with various cellular activities (AAA) {ECO:0000313|EMBL:EFP58972.1};
GN   Name=clpC {ECO:0000313|EMBL:EFP58972.1};
GN   ORFNames=HMPREF0321_2069 {ECO:0000313|EMBL:EFP58972.1};
OS   Dermacoccus sp. Ellin185.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Dermacoccus.
OX   NCBI_TaxID=188626 {ECO:0000313|EMBL:EFP58972.1, ECO:0000313|Proteomes:UP000003057};
RN   [1] {ECO:0000313|EMBL:EFP58972.1, ECO:0000313|Proteomes:UP000003057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin185 {ECO:0000313|EMBL:EFP58972.1,
RC   ECO:0000313|Proteomes:UP000003057};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {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:EFP58972.1}.
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DR   EMBL; AEIQ01000042; EFP58972.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3B7D7; -.
DR   eggNOG; COG0542; Bacteria.
DR   Proteomes; UP000003057; 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; 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: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; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
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   REGION          147..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          829..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   874 AA;  95413 MW;  AF3A94365B5684B3 CRC64;
     MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKALE SLGISLDAVR
     EQVQEIIGQG QQTQSGHIPF TPRAKKVLEL SLREGLQLGH SYIGTEHILL GLIREGEGVA
     AQVLVKLGAD LSTVRTTVIQ LLSGYQGKGE PQAAGVGASS SGGPAEGTPA GSTVLDQFGR
     NLTQAAREGK LDPVIGREKE IERVMQVLSR RTKNNPVLIG EPGVGKTAVV EGLAADIVAG
     DVPETLKDKH LYTLDLGSLV AGSRYRGDFE ERLKKVLKEI RTRGDIILFI DEIHSLVGAG
     AAEGAIDAAS ILKPMLARGE LQTIGATTLD EYRKHIEKDA ALERRFQPIQ VNEPTIPQAI
     EILKGLRDRY EAHHRVTITD AALVGAVNMA DRYITDRFLP DKAIDLIDEA GARLRIRRMT
     APPELREFDE KIVHVRREKE SAIDSQDFEK AAALRDDERK LVEEKEAKEK EWKAGDVDLA
     AVLDEELVAE VLAASTGIPV FKLTEEESSR LLRMEDELHK RVIGNDDAIK ALSQAIRRTR
     AGLKDPRRPG GSFIFAGPTG VGKTELAKSL AEFLFGDEDA LITLDMSEYA EKHTVSRLFG
     SPPGYVGYEE GGQLTEKVRR KPFSVVLFDE VEKAHADIFN SLLQILEDGR LTDSQGRVVD
     FKNTVIIMTT NLGTRDIAKG VSLGFAAGND QRSNYDRMKA KVGEELKQHF RPEFLNRVDD
     TIVFPQLSQA EIVEIVDLMV AKLDERLKDQ DMAIELTQGA KDLLAKRGYD PALGARPLRR
     TIQREIEDQL SEKILFGEIS KGDLVLVDVE GEGKEATFTF SGTPISLSKH TRASDKVDTD
     MKGATPSSDD LSGPIDFGGA VGGGPGGGEG AAAV
//
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