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Database: UniProt
Entry: A5GLZ6_SYNPW
LinkDB: A5GLZ6_SYNPW
Original site: A5GLZ6_SYNPW 
ID   A5GLZ6_SYNPW            Unreviewed;       844 AA.
AC   A5GLZ6;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpA homolog {ECO:0000313|EMBL:CAK23961.1};
GN   Name=clpA {ECO:0000313|EMBL:CAK23961.1};
GN   OrderedLocusNames=SynWH7803_1535 {ECO:0000313|EMBL:CAK23961.1};
OS   Synechococcus sp. (strain WH7803).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=32051 {ECO:0000313|EMBL:CAK23961.1, ECO:0000313|Proteomes:UP000001566};
RN   [1] {ECO:0000313|Proteomes:UP000001566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7803 {ECO:0000313|Proteomes:UP000001566};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CT971583; CAK23961.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5GLZ6; -.
DR   STRING; 32051.SynWH7803_1535; -.
DR   KEGG; syx:SynWH7803_1535; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_3; -.
DR   Proteomes; UP000001566; 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   Hydrolase {ECO:0000313|EMBL:CAK23961.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CAK23961.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001566};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT   DOMAIN          1..131
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          407..442
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          447..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  92890 MW;  31790D14F4493AD8 CRC64;
     MLAQEEARRL GHNFVGTEQI LLGLIGEGTG VAAKVLKSMG VNLKDARVEV EKIIGRGSGF
     VAVEIPFTPR AKRVLELSLE EARQLGHNYI GTEHLLLGLI REGEGVAARV LENLGVDLSK
     VRTQVIRMLG ETAEVGAGGS GSGSKGSTKT PTLDEFGNNL TQLAGEAKLD PVVGRQSEID
     RVIQILGRRT KNNPVLIGEP GVGKTAIAEG LAQRIQQGDI PDILEDKRVL TLDIGLLVAG
     TKYRGEFEER LKKIMEEIKA AGNVILVIDE VHTLIGAGAA EGAIDAANIL KPALARGELQ
     CIGATTLDEY RKHIERDAAL ERRFQPVTVG EPSIDDTIEI LKGLRERYEQ HHRLRITDEA
     LEAAATLGDR YISDRFLPDK AIDLIDEAGS RVRLMNSKLP PEAKEVDKEL RAVQKEKEDA
     VREQDFSRAG ELRDKEVELR DKIRSLLQSS REDSPSDNQQ SEDQATDVDV ASTESEGATE
     LAVTGTTPVV NEEDIAQIVA SWTGVPVQKL TESESVKLLN MEETLHKRLI GQDEAVKAVS
     KAIRRARVGL KNPNRPIASF IFSGPTGVGK TELTKALAAY FFGSEEAMIR LDMSEFMERH
     TVSKLIGSPP GYVGFNEGGQ LTEAVRRRPY TVVLFDEIEK AHPDVFNLLL QLLEDGRLTD
     SKGRTVDFKN TLIIMTSNIG SKVIEKGGGG LGFEFSGENA EENQYNRIRS LVNEELKQYF
     RPEFLNRLDE IIVFRQLNRD EVKEIAEIML REVFGRIGEK GITLTVSDAF KERLVEEGYN
     PAYGARPLRR AVMRLLEDSL AEEVLSGRIK DGDEAEVDVE DGKVVVKHLN RTATETPELA
     SAGR
//
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