ID A0A2P7EEZ8_9SYNE Unreviewed; 844 AA.
AC A0A2P7EEZ8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:PSI01832.1};
GN ORFNames=C7K08_05975 {ECO:0000313|EMBL:PSI01832.1};
OS Synechococcus lacustris str. Tous.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1910958 {ECO:0000313|EMBL:PSI01832.1, ECO:0000313|Proteomes:UP000240206};
RN [1] {ECO:0000313|Proteomes:UP000240206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tous {ECO:0000313|Proteomes:UP000240206};
RA Cabello-Yeves P.J., Picazo A., Camacho A., Callieri C., Rosselli R.,
RA Roda-Garcia J., Coutinho F.H., Rodriguez-Valera F.;
RT "Ecological and genomic features of two cosmopolitan and abundant
RT freshwater picocyanobacteria.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:PSI01832.1}.
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DR EMBL; PXVC01000018; PSI01832.1; -; Genomic_DNA.
DR STRING; 1910958.BTM30_02680; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000240206; 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; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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 Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Hydrolase {ECO:0000313|EMBL:PSI01832.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PSI01832.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000240206};
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 417..452
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 460..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 93036 MW; 99C5C9D8BAB4FEA8 CRC64;
MFERFTEKAI KVIMLAQEEA RRLGHNFVGT EQILLGLIGE GTGVAAKVLK SMGVNLKDAR
VEVEKIIGRG SGFVAVEIPF TPRAKRVLEL SLEEARQLGH NYIGTEHLLL GLIREGEGVA
ARVLENLGVD LAKVRTQVIR MLGETAEVSA GGGSKGSTKT PTLDEFGSNL TQLASDGKLD
PVVGRQNEIE RVIQILGRRT KNNPVLIGEP GVGKTAIAEG LAQRIIDGEV PDILEEKRVL
TLDIGLLVAG TKYRGEFEER LKKIMEEIRG AGNVILVIDE VHTLIGAGAA EGAIDAANIL
KPALARGELQ CIGATTLDEY RKHIERDAAL ERRFQPVMVG EPSVAETIEI LRGLKERYET
HHRLKISDDA LIAAATLGDR YISDRFLPDK AIDLVDEAGS RVRLLNSKLP PAAKELDKQL
RAVQKXKELA VREQNYTKAG ELRDKEVELR EQVRGITQAR RDEIAASNEA PADGEXAKPA
ETTTDGTPVV SEEDIAQIVA SWTGVPVQKL TETESAKLLN MEETLHQRLI GQDEAVKAVS
KAIRRARVGL KNPNRPIASF IFSGPTGVGK TELTKALAAY FFGSEESMIR LDXSEFMERH
TVSKLIGSPP GYVGFNEGGQ LTEAVRRRPY TVVLFDEIEK AHPDVFNLLL QLLEDGRLTD
SKGRTVDFKN TLIIMTSNIG SKVIEKGGGG LGFEFGGGDV EENQYNRIRS LVNEELKQYF
RPEFLNRLDE IIVFRQLNRD EVKLIADIML REVFTRMQEK GISLSVTESF KERLVEEGYN
PSYGARPLRR AVMRLLEDSL AEEFLSGRLK DGDAALVDVN EDKQVVIRQT TLPQEQPELA
SAGV
//