ID A0A1Q8ZF31_9CYAN Unreviewed; 826 AA.
AC A0A1Q8ZF31;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:OLP18896.1};
GN ORFNames=BST81_08245 {ECO:0000313|EMBL:OLP18896.1};
OS Leptolyngbya sp. 'hensonii'.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya.
OX NCBI_TaxID=1922337 {ECO:0000313|EMBL:OLP18896.1, ECO:0000313|Proteomes:UP000186296};
RN [1] {ECO:0000313|EMBL:OLP18896.1, ECO:0000313|Proteomes:UP000186296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=hensonii {ECO:0000313|Proteomes:UP000186296};
RA Hamilton T.L., Klatt J.M., De Beer D., Macalady J.;
RT "Physiology of photosynthesis in the novel isolate Oscillatoriales
RT cyanobacterium hensonii.";
RL Submitted (NOV-2016) 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:OLP18896.1}.
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DR EMBL; MQTZ01000020; OLP18896.1; -; Genomic_DNA.
DR RefSeq; WP_075598071.1; NZ_MQTZ01000020.1.
DR AlphaFoldDB; A0A1Q8ZF31; -.
DR STRING; 1922337.BST81_08245; -.
DR OrthoDB; 438311at2; -.
DR Proteomes; UP000186296; 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 Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Hydrolase {ECO:0000313|EMBL:OLP18896.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:OLP18896.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186296};
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 422..457
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
SQ SEQUENCE 826 AA; 91162 MW; 5F56B3A3EE77A07A CRC64;
MFELFTDKAI KAVMIAQEEA RRLKHNFVGT EQILLGVIGE QTSVAAQVLT QLGVTFQEAR
LEVERIIGQG AGFVPPEIPF TPKVKRVFEQ ALQEARQLGD RYVTPEHLLL GITVESDGVA
LRVLENLKVD ISTLRAEIAK ALEELAAVPM GSAPERSPRQ ASSREMTTLE EFGTNLTQLA
VQGKLDPVIG REKEIERVIQ ILGRRTKNNP VLIGEPGVGK TAIAEGLAQR IVNQDVPEAL
EDKQVIGLDM GRLLAGTRYR GDFEDRLSKI IEEVRSNNNI ILVIDEIHTL VGAGAIGGGM
DAANMLKPAL ARGELQCLGA TTLDEYRQHI EQDAALERRF QSVMVGEPTV AETIEILFGL
RERYEQHHRI EISDAALVAA AQLADRYIAD RFLPDKAIDL IDEAGSRVRL AHTQSSLSKE
LKQQLRQVIR EKSEAVQTQD FVKAAQLRDR ELELEAQLQS DSTVGSTSLR LPVVTEEDIA
QIVGAWTGIP VTKLTESETV RLLHLEDTLH QRVIGQHEAV KAVARSLRRA SVGLKHPNRP
IASFIFSGPT GVGKTELAKA LAHYFFGSQE SMIRLDMSEF MESHTVSKLI GSPPGYVGYG
EGGQLTEAVR RKPYTVLLFD EVEKAHPEVF NLLLQLLEDG RLTDAQGRIV SFKNTLVIMT
SNIGSRVIEK GGGGLGFEVG GDIAEAQYNR IRTLVNEDLK QHFRPEFLNR LDDIIVFQSL
VREEVKQIAD LMIREVGDRL REQSIALQVT ELFKDLLLRE GFSPAYGARS LRRAITRLLE
DALAEALLTG RIGAGDTAIV DVDVDGDGLV VVRRDATLEA RLPATV
//