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Database: UniProt
Entry: A0A368VY57_9ACTN
LinkDB: A0A368VY57_9ACTN
Original site: A0A368VY57_9ACTN 
ID   A0A368VY57_9ACTN        Unreviewed;       854 AA.
AC   A0A368VY57;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:RCW46300.1};
GN   ORFNames=DFQ14_102603 {ECO:0000313|EMBL:RCW46300.1};
OS   Halopolyspora algeriensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetes incertae sedis;
OC   Halopolyspora.
OX   NCBI_TaxID=1500506 {ECO:0000313|EMBL:RCW46300.1, ECO:0000313|Proteomes:UP000253495};
RN   [1] {ECO:0000313|EMBL:RCW46300.1, ECO:0000313|Proteomes:UP000253495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8575 {ECO:0000313|EMBL:RCW46300.1,
RC   ECO:0000313|Proteomes:UP000253495};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUL-2018) 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:RCW46300.1}.
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DR   EMBL; QPJC01000002; RCW46300.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368VY57; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000253495; 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};
KW   Hydrolase {ECO:0000313|EMBL:RCW46300.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RCW46300.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253495};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          39..180
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          458..493
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          162..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   854 AA;  93361 MW;  A9D96687D697B7B0 CRC64;
     MATFFGPGGF ERGFFDEYLA GLFGADRATP GSGRRVDITE LMTQQTQQLL DEAAGYARER
     GHTDLDALHL LWAAARNAHT RGMLEAAGVD PDGFAGAVQE QLPPARDGER RQAPSLTAAG
     KKVLVDAYQV ARALGSTYIG PDHVLLAMSA AQDSQVGRLL GAAGASPEDL RSSEGSAQHP
     AAQHPSAQQS GQQQRGESAT PTLDQYGQDL TARARGGELD PVIGRETEIG QTIEVLSRRT
     KNNPVLVGEA GVGKTAIVEG IAQRIADGRV PKVLAGKRVV QLDLSGMLAG TRYRGDFEER
     MTKVIEEIGS NSDEIIVFLD ELHTVVGAGG AEGAVDAGNM LKPRLARGEL HVVGATTLDE
     YRKNIEKDAA LERRFQPVQV DEPTVEDTIA VLSRLKERYQ DHHRVHYTEE AVDAAARLSD
     RYLTDRFLPD KAIDLMDQAG ARKRLQELTP AEDAQQLQQR IDQLTRDKDR AVAEERYEHA
     SRLRDEIGVA QAELAANSAD DTVRDGEVAE VTATDIAEVV SRSTGVPVSR MTEEEKARLQ
     RLEEELHQRV VGQDDAVRAL ARSVRRSRSG MGNPNRPVGS FLFLGPTGVG KTELAKALAE
     TMFGDESRMV RLDMSEFQER HTASRLVGAP PGYVGYGEAG ELTEAVRRRP YSVVLLDEIE
     KAHTDVFNTL LQVLEDGRLT DGQGRTVDFT NTVLIMTSNL GSEIISSRSG RLGFSSPEQQ
     GSDEPLRERL MPRLREEFRP EFLNRIDDVV VFRKLGTEQL HTITNLLLDD TRQRLQAMDI
     EVEFSTGAID WIAERGHQPE FGARPLRRTI EHEIDDRIAD LVLDGDLNAG DRLRVDAGAE
     GPLLAVDAAA TASA
//
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