ID K9SPY6_9SYNE Unreviewed; 828 AA.
AC K9SPY6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=ATPase with chaperone activity, ATP-binding subunit {ECO:0000313|EMBL:AFY72200.1};
GN ORFNames=Syn7502_00025 {ECO:0000313|EMBL:AFY72200.1};
OS Synechococcus sp. PCC 7502.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1173263 {ECO:0000313|EMBL:AFY72200.1, ECO:0000313|Proteomes:UP000010385};
RN [1] {ECO:0000313|EMBL:AFY72200.1, ECO:0000313|Proteomes:UP000010385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7502 {ECO:0000313|EMBL:AFY72200.1,
RC ECO:0000313|Proteomes:UP000010385};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Synechococcus sp. PCC 7502.";
RL Submitted (MAY-2012) 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; CP003594; AFY72200.1; -; Genomic_DNA.
DR RefSeq; WP_015166859.1; NC_019702.1.
DR AlphaFoldDB; K9SPY6; -.
DR STRING; 1173263.Syn7502_00025; -.
DR KEGG; synp:Syn7502_00025; -.
DR PATRIC; fig|1173263.3.peg.25; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_3; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000010385; 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 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|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000010385};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT DOMAIN 2..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 416..451
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 412..461
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 828 AA; 91930 MW; CDFCDEA31106C3E0 CRC64;
MFERFTEKAI KVIMLAQEEA RRLGHNFVGT EQILLGLIGE GTGVAAKVLK SMGVNLKDAR
IEVEKIIGRG SGFVAVEIPF TPRAKRVLEL SLEEARQLGH NYIGTEHLLL GLIREGEGVA
ARVLENLGVD LSKVRTQVIR MLGETAEVSA GGGGGRTKTP TLDEFGSNLT QLAMEGKLDP
VVGRQKEIER VIQILGRRTK NNPVLIGEPG VGKTAIAEGL AQRITSGDIP DILQDKRVVT
LDIGLLVAGT KYRGEFEERL KKIMDEIRSS NNVILVIDEV HTLIGAGAAE GAIDAANILK
PALARGELQC IGATTLDEYR KHIERDAALE RRFQPVMVGE PSVEETIEIL FGLRERYEQH
HKLKISDLAI DAAAKLSDRY ISDRFLPDKA IDLIDEAGSR VRLLNSQLPP AAKELDKELR
QLLKDKDDAV RSQDFDKAAK LRDRELEIKQ EIRNLSQAKK AETTKDDVVP VVTEEDIAHI
VSSWTGVPVS KLTESESLKL MQMEETLHQR LIGQEEAVKA TSRAIRRARV GLKNPNRPIA
SFIFSGPTGV GKTELTKALA AYFFGSEEAM VRLDMSEFME RHTVSKLIGS PPGYVGYNEG
GQLTEAVRRR PYTVILFDEI EKAHPDVFNL LLQILEDGRL TDSKGRTVDF KNTLIIMTSN
IGSKVIEKGG GGLGFDFAED QADSAYTRIR SLVNEELKQY FRPEFLNRLD EIIVFRQLKI
EEIREIAELM LNEVYKRLKE KNITLAVTER FKDLLVREGY NQSYGARPLR RAIMRLLEDS
LSEEILTGKV RDGASVIVDV DDDGKVICVE QPSAIAPADS PLQLMPSA
//
