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Database: UniProt
Entry: A0A0C1QU86_9CYAN
LinkDB: A0A0C1QU86_9CYAN
Original site: A0A0C1QU86_9CYAN 
ID   A0A0C1QU86_9CYAN        Unreviewed;       821 AA.
AC   A0A0C1QU86;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:KAF3885303.1};
DE   SubName: Full=Clp protease ClpX {ECO:0000313|EMBL:KIE09004.1};
GN   ORFNames=DA73_0231555 {ECO:0000313|EMBL:KIE09004.1}, DA73_0400007405
GN   {ECO:0000313|EMBL:KAF3885303.1};
OS   Tolypothrix bouteillei VB521301.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE09004.1};
RN   [1] {ECO:0000313|EMBL:KIE09004.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VB521301 {ECO:0000313|EMBL:KIE09004.1};
RX   PubMed=25700407;
RA   Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA   Adhikary S.P., Tripathy S.;
RT   "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL   Genome Announc. 3:e00001-15(2015).
RN   [2] {ECO:0000313|EMBL:KAF3885303.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VB521301 {ECO:0000313|EMBL:KAF3885303.1};
RA   Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA   Tripathy S.;
RT   "Improved Assembly of Tolypothrix boutellei genome.";
RL   Submitted (NOV-2019) 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:KIE09004.1}.
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DR   EMBL; JHEG04000001; KAF3885303.1; -; Genomic_DNA.
DR   EMBL; JHEG02000058; KIE09004.1; -; Genomic_DNA.
DR   RefSeq; WP_038087343.1; NZ_JHEG04000001.1.
DR   AlphaFoldDB; A0A0C1QU86; -.
DR   STRING; 1479485.DA73_0231555; -.
DR   OrthoDB; 438311at2; -.
DR   Proteomes; UP000029738; 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:SF155; CLP PROTEASE ATP-BINDING SUBUNIT; 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   Hydrolase {ECO:0000313|EMBL:KIE09004.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KIE09004.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029738};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT   DOMAIN          2..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          420..455
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
SQ   SEQUENCE   821 AA;  90786 MW;  6113A07E9A498A26 CRC64;
     MFEHFTSEAI KVIMLAQEEA RRLGHNFVGT EQILLGLIGE GTGVAAKVLT DLGVTLKDAR
     REVERIIGRG SGFVPPEIPF TPKVKSLFEQ AFKEARSLGH NYISTEHLLL GLTEAGEGVA
     AKVLQNLGLD LSQVRTAVIR NLGEATSVSG SRVGSSNGQR RNQSLTLEEF GKNLTKLAKE
     GKLDPVVGRE KEIERAVQIL GRRTKNNPVL IGEPGVGKTA IAEGLAQRIV NQDIPDILQD
     KQVISLDMGL LVAGTRFRGD FEERLKKIMD EIRSSGNIIL VIDEIHTLVG AGGTEGGMDA
     ANILKPALAR GELQCIGATT LDEYRKHIER DAALERRFQP IMIGEPSVEE TIEILYGLRS
     AYESHHRVQI SDEALVAAAK LSDRYISDRF LPDKAIDLID EAGSRVRLRY SSNPANREIK
     KELARVSKSK DEAVRMQDFD KAGELRDREL ELEAQLREIS QNDKAVNSPI VDEEDIAQIV
     ASWTGVPVNK LTESESELLL HLEDTLHQRL IGQEQAVTAV SRAIRRARVG LKNPNRPIAS
     FIFSGPTGVG KTELTKALAS YFFGSEDAMI RLDMSEYMER HTVSKLIGSP PGYVGFDEGG
     QLTEAVRRKP YTVVLFDEIE KAHPDVFNML LQILEDGRLT DAKGRTVDFK NTLIIMTSNI
     GSKVIEKGGG GLGFQFADDA AEASYNRIRS LVNEELKSFF RPEFLNRLDE IIVFTQLKKD
     EIKQIADIML REVASRLTEK GISLEVSDRF KERVIQEGYD PSYGARPLRR AIMRLLEDSL
     AEAMLSGEIA EGDTANVDVD DDGQVKVTKS QSRELLLANL G
//
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