ID A0A2W1JGT4_9CYAN Unreviewed; 824 AA.
AC A0A2W1JGT4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:PZD70835.1};
GN Name=clpC_3 {ECO:0000313|EMBL:PZD70835.1};
GN ORFNames=C1752_08977 {ECO:0000313|EMBL:PZD70835.1};
OS Acaryochloris thomasi RCC1774.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris; Acaryochloris thomasi.
OX NCBI_TaxID=1764569 {ECO:0000313|EMBL:PZD70835.1, ECO:0000313|Proteomes:UP000248857};
RN [1] {ECO:0000313|EMBL:PZD70835.1, ECO:0000313|Proteomes:UP000248857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC1774 {ECO:0000313|EMBL:PZD70835.1,
RC ECO:0000313|Proteomes:UP000248857};
RX PubMed=29904088; DOI=10.1038/s41598-018-27542-7;
RA Partensky F., Six C., Ratin M., Garczarek L., Vaulot D., Probert I.,
RA Calteau A., Gourvil P., Marie D., Grebert T., Bouchier C., Le Panse S.,
RA Gachenot M., Rodriguez F., Garrido J.L.;
RT "A novel species of the marine cyanobacterium Acaryochloris with a unique
RT pigment content and lifestyle.";
RL Sci. Rep. 8:9142-9142(2018).
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:PZD70835.1}.
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DR EMBL; PQWO01000027; PZD70835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1JGT4; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000248857; 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 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.
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:PZD70835.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PZD70835.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248857};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 2..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 824 AA; 91118 MW; 350C4882945C4BDE CRC64;
MFECFTEKAI KVIMLAQEES HRLKQMFVGT ELILLGLIGE ETGIAATVLK SLGANLPKAR
LDVEKSVGKG SSPVKAEITF TPRSKRVLES ALEESRQLGH SYVGTEHLLL ALIKDEQGVA
AQVLLNLEID VIDIRTRVMQ RLSEPTAVPS GNRPTVQRNY NFPKRSTLDE FGTNLTQLAV
EGSLDPVVGR QTEVQRMIQI LNRRTKNNPI LIGEPGVGKT ALAEGLAQRI VNHDVPDAIE
GKCVFTLNVG SLLAGTKYRG EFEERLKAIV EEVRSSGNII LVIDEIHTLV GSGAAEGGLD
AANILKPSLA RGELQCIGAT TLDDYRQYIE RDSALERRFQ PVMVNESSVE ETIEILKGLR
SCYEQHHQLE ISDLALEAAA KLSDRYICDR FLPDKAIDLI DEAGSKIRIS SSKAASTDKK
LSKELRQILK EKGNATQKQD YSLARELRIR EVEIQNKLQG DSQTLFSNPA DLILPIVNEE
DIASIVASWT GVPVNKLTES ESENLLQLED ILHQRIIGQE EAVKAVSRAM RRVRTGLKDP
NRPIASFIFS GPTGVGKTEL AKALASSYFG SEAAMIRLDM SEYMESHTVA KLVGSPPGYI
GFDEGGQLTE AVRRQPYTVV LFDEIEKAHP DVFNLLLQVL EDGRLTDAKG RTVDFKNTLL
IMTSNVGSKV IQKGGSGLGF EFSDDLAGAQ YSRIVSVVNE ELKQFFRPEF LNRLDEIIVF
QQLNKTEVRQ IADILLHEVF ARVAERRIAV EVTDLFKERL VETGYDPEMG ARPLRRAITR
LLEDCLAEEI LTGRVKTGDA VIVDVNGAGQ TQVLIKQVER SGCK
//