ID A3Z3D8_9SYNE Unreviewed; 913 AA.
AC A3Z3D8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Putative ATP-dependent Clp protease, Hsp 100, ATP-binding subunit ClpB {ECO:0000313|EMBL:EAQ70482.1};
GN ORFNames=RS9917_06585 {ECO:0000313|EMBL:EAQ70482.1};
OS Synechococcus sp. RS9917.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=221360 {ECO:0000313|EMBL:EAQ70482.1, ECO:0000313|Proteomes:UP000005593};
RN [1] {ECO:0000313|EMBL:EAQ70482.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS9917 {ECO:0000313|EMBL:EAQ70482.1};
RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (JAN-2006) 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:EAQ70482.1}.
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DR EMBL; AANP01000001; EAQ70482.1; -; Genomic_DNA.
DR RefSeq; WP_007101293.1; NZ_CH724158.1.
DR AlphaFoldDB; A3Z3D8; -.
DR STRING; 221360.RS9917_06585; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_3; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000005593; 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:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 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, ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:EAQ70482.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EAQ70482.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT DOMAIN 19..158
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 152..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 454..564
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 161..199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 100818 MW; 40E10F185878B971 CRC64;
MLPEDRPAID SPVSLTSEPD RFSDEAWELL LAGQDLARRW RHGELDVEHL MQVLFSDRRF
AGSLRGLSLD ADDLLDQLEG FLAEQPMARS EDLFIGEDLE QLLEAADRVR ALWGSRLIEL
SHLLIAMGRD PRIGADCLAS AGLPADRLES ELRRQRPTAA AAPVPPAPPA PTPAPPLPPP
PAAPAPPPVQ APAPASPEPE EPSALQLYGR DLTAAAEAGQ LDPVIGRDGE IRRLIKVLSR
RGKNNPVLIG APGVGKTAIA ECLAQRIVAG EVPDSLRGQR LVALDMGALI AGAKFRGQFE
ERLRSVLAEV SDADAGVVLF IDELHTVVSS DRSSADAGSL LKPALARGEL RCIAATTPED
YRRTVEKDPA LSRRFQQVPI LEPSIELSIE ILRGLKERYE LHHGVTITDG ALTAAARLAD
RYISDRCLPD KAIDLIDEAA AQLKMDVTSK PQVVEDAETD LRRVELALLA AEQAPEAERV
QLQRSRLEAS ACLEDLRGRW QAERDQLEEL RQLLQEDETL RHAIAEAERN GDLEEAARLE
YDQLHRVQQR RTDLEQVLVE AQEQGTALLR EQVEAGDIAD VVARWTGIPV QRLLAGERQK
LLELETQLQQ RVIGQPEAVQ AVASAIRRAR AGMKDPRRPV GSFLFLGPTG VGKTELAKAL
AARLFDEEEA LVRLDMSEFM ERNAVARLLG APPGYVGYEE GGQLTEAVRR RPYALLLLDE
VEKAHPDVFN VLLQVLDDGR LTDSQGRTVD FRHTVVVMTS NLASRAILDR AREGQQPDAD
QAALDQALAV RVDEALARQF RPEFLNRIDE VIRFRPLAIE DLERIVHLQL AELAQLMREQ
DLELRVDPAV VRALAEQGFE PEYGARPLRR VLRRQLENPL ATQLLEDRFS GASAVRVRSG
DGALEPFLFT PED
//
