ID A0A077JBV6_9CYAN Unreviewed; 823 AA.
AC A0A077JBV6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=ATP-dependent Clp protease regulatory subunit {ECO:0000313|EMBL:BAP16974.1};
GN Name=clpC {ECO:0000313|EMBL:BAP16974.1};
GN ORFNames=ETSB_0074 {ECO:0000313|EMBL:BAP16974.1};
OS cyanobacterium endosymbiont of Epithemia turgida isolate EtSB Lake Yunoko.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=1228987 {ECO:0000313|EMBL:BAP16974.1, ECO:0000313|Proteomes:UP000031625};
RN [1] {ECO:0000313|EMBL:BAP16974.1, ECO:0000313|Proteomes:UP000031625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ETSB Lake Yunoko {ECO:0000313|EMBL:BAP16974.1};
RX PubMed=25049384; DOI=10.1073/pnas.1405222111;
RA Nakayama T., Kamikawa R., Tanifuji G., Kashiyama Y., Ohkouchi N.,
RA Archibald J.M., Inagaki Y.;
RT "Complete genome of a nonphotosynthetic cyanobacterium in a diatom reveals
RT recent adaptations to an intracellular lifestyle.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11407-11412(2014).
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}.
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DR EMBL; AP012549; BAP16974.1; -; Genomic_DNA.
DR RefSeq; WP_044105586.1; NZ_AP012549.1.
DR AlphaFoldDB; A0A077JBV6; -.
DR STRING; 1228987.ETSB_0074; -.
DR KEGG; ceo:ETSB_0074; -.
DR HOGENOM; CLU_005070_4_1_3; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000031625; Chromosome.
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 Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Hydrolase {ECO:0000313|EMBL:BAP16974.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:BAP16974.1};
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 418..453
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
SQ SEQUENCE 823 AA; 91309 MW; 3AE07F3346E34BBC CRC64;
MFERFTEKAI KVIMLAQEEA RRLGHNFVGT EQILLGLIGE GTGVAAKVLK SMGINLKDAR
VEVEKIIGRG SGFVAVEIPF TPRAKRVLEL SLEEARQLGH NYIGTEHLLL GLIREGEGVA
ARVLENLGVD LSKVRTQVIR QLGETAEVAA GGGPSGRSNK TPTLDEFGSN LTNMAGEGKL
DPVVGRHKEI ERVIQILGRR TKNNPVLIGE PGVGKTAIAE GLAQRIATKD VPDILEEKRV
VTLDIGLLVA GTKYRGEFEE RLKKIMDEIR QAGNVILVID EVHTLIGAGA AEGAIDAANI
LKPALARGEL QCVGATTLDE YRKHIERDAA LERRFQPVMV GEPSVDETIE ILYGLRERYE
QHHKLKILDE ALEAAAKLSD RYISDRYLPD KAIDLIDEAG SRVRLINSQL PPAAKELDKE
LRSILKQKDD AVRAQDFDKA GELRDREMEI KEEIRSISSA KKTEGDSDDP FVDSEEIAHI
VASWTGVPVN KLTESESEKL LHMEDTLHQR LIGQEDAVKA VSRAIRRARV GLKNPGRPIA
SFVFSGPTGV GKTELTKALA AYFFGSEDAM VRLDMSEYME RHTVSKLIGS PPGYVGYNEG
GQLTEAVRRR PYTVILFDEI EKAHPDVFNM LLQILEDGRL TDAKGRTVDF KNTLLIMTSN
IGSKVIEKGG GGLGFEFEEN KTEAQYNRIR ALVNEELKNY FRPEFLNRLD EIIVFRQLDK
NEVKEISEIL LKEVFARLTD KNITLNVTEK FKERLVEEGY NPAYGARPLR RAIVRLLEDI
LAEEILSGRV SEGDAALVDI DADGKVKVIS SENKEDLLAK TTD
//