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Database: UniProt
Entry: A0A5J6Q6F0_9SYNE
LinkDB: A0A5J6Q6F0_9SYNE
Original site: A0A5J6Q6F0_9SYNE 
ID   A0A5J6Q6F0_9SYNE        Unreviewed;       967 AA.
AC   A0A5J6Q6F0;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=AAA family ATPase {ECO:0000313|EMBL:QEY32796.1};
GN   ORFNames=EVJ50_11705 {ECO:0000313|EMBL:QEY32796.1};
OS   Synechococcus sp. RSCCF101.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=2511069 {ECO:0000313|EMBL:QEY32796.1, ECO:0000313|Proteomes:UP000325996};
RN   [1] {ECO:0000313|EMBL:QEY32796.1, ECO:0000313|Proteomes:UP000325996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSCCF101 {ECO:0000313|EMBL:QEY32796.1,
RC   ECO:0000313|Proteomes:UP000325996};
RA   Ng Y.M., Mokhtar N.A., Jamhor S.A., Gojobori T., Archer J.A.C.;
RT   "Genome of Synechococcus sp. RSCCF101.";
RL   Submitted (FEB-2019) 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}.
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DR   EMBL; CP035632; QEY32796.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5J6Q6F0; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000325996; 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; -; 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 104; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000325996};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          20..161
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          160..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          531..623
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        242..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   967 AA;  106599 MW;  C29D2C2C48C65698 CRC64;
     MVLAEDARDS GLGTSLTAEP ERFSEAAWDL VLASQDVARR WRHGQMDVEH LLQALFTDPR
     YEGWVLDLPL QADPLLDRLE DFCADQPSGR GEALYIGEAL ELLLEDADRC RAGWGSRLID
     VPHLMLALLE EPRIGAALLT EAGLSEEALL RQLRRTGPRV PVQREVERPE QVPSPPEPSQ
     SEPSPVGVRR PPTRPAGPRS RPDAAGAPMA AAPPDDWIDG RGRPARASVG EAPPSGAADP
     SEPSGEDDRL QPEPSALDRF GRDLTDAARQ GQLDPVIGRD AEIRRLIQVL SRRGKNNPVL
     IGDPGVGKTA VAELLAQRIV AGEVPESLQG LRLVALDLGA LIAGAKFRGQ FEERLRAVLA
     EVSDPDAGVV LFIDELHTVV RSDRSSADAG SLLKPALARG ELRCIAATTS EEYGRTVEKD
     PALSRRFQQV LIREPSPAVS HEILRGVRER YELHHGLTIS DAALAAATRL ADRYISDRCL
     PDKAIDLVDE AAAQLKMDVT SKPRVVEEAE AALRQADLDR IAAEDGPEDQ RLRQQEQHRA
     AQEALDRLID RWEAERDQLA DLRALQHEEE DLRHAIAEAD RAGDHEEAAR LQIDRLQDVQ
     DRRRDLEARL AEAQRRGEAL LRDQVEEGDI ADVVARWTGI PVQRLMAGER QKLLHLDERL
     GERVIGQPEA VAAVAAAIRR ARAGMKDPRR PVGSFLFLGP TGVGKTELAK ALADALFDEE
     EALVRLDMSE FMERNAVARL LGAPPGYVGY EEGGQLTEAV RRRPYAVLLL DEVEKAHPDV
     FNVLLQLLDD GRLTDSQGRT VDCRNTVVVM TSNLASRAIL ERARQPGGAE QDAALEAAVD
     QALASHFRPE FLNRIDEVIR FRPLQPQDLE RIVRLQLADL DRLLQEQGLR LEVVDPVVTA
     LAEEAYEPEY GARPLRRLLR RRLENPLATA LLEDTFHGAV AVRVEPGEDT RSLETLRFLP
     VAAPGTS
//
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