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Database: UniProt
Entry: A4CVJ2_SYNPV
LinkDB: A4CVJ2_SYNPV
Original site: A4CVJ2_SYNPV 
ID   A4CVJ2_SYNPV            Unreviewed;       857 AA.
AC   A4CVJ2;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 93.
DE   SubName: Full=ATPase {ECO:0000313|EMBL:EAR18013.1};
GN   ORFNames=WH7805_04456 {ECO:0000313|EMBL:EAR18013.1};
OS   Synechococcus sp. (strain WH7805).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=59931 {ECO:0000313|EMBL:EAR18013.1, ECO:0000313|Proteomes:UP000001224};
RN   [1] {ECO:0000313|EMBL:EAR18013.1, ECO:0000313|Proteomes:UP000001224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7805 {ECO:0000313|Proteomes:UP000001224};
RA   Scanlan D., Ostrowski M., Mazard S., Wilkinson N., Partensky F.,
RA   Dufresne A., Garczarek L., Hess W., Gierga G., Voss B., Axmann I., Post A.,
RA   Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K., Beeson K.,
RA   Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-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:EAR18013.1}.
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DR   EMBL; AAOK01000004; EAR18013.1; -; Genomic_DNA.
DR   RefSeq; WP_006041704.1; NZ_CH724168.1.
DR   AlphaFoldDB; A4CVJ2; -.
DR   STRING; 59931.WH7805_04456; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_3; -.
DR   OMA; ERMKAVM; -.
DR   OrthoDB; 9803641at2; -.
DR   PhylomeDB; A4CVJ2; -.
DR   Proteomes; UP000001224; 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   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   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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
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          421..456
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          419..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   857 AA;  94493 MW;  D4CE9E2C6273FBA9 CRC64;
     MFERFTEKAI KVIMLAQEEA RRLGHNFVGT EQILLGLIGE GTGVAAKVLK SMGVNLKDAR
     VEVEKIIGRG SGFVAVEIPF TPRAKRVLEL SLEEARQLGH NYIGTEHLLL GLIREGEGVA
     ARVLENLGVD LAKVRTQVIR MLGETAEVGA GGGSGSGAKG STKTPTLDEF GNNLTQLAGE
     AKLDPVVGRH NEIDRVIQIL GRRTKNNPVL IGEPGVGKTA IAEGLAQRIQ QGDIPDILED
     KRVLTLDIGL LVAGTKYRGE FEERLKKIME EIKSAGNVIL VIDEVHTLIG AGAAEGAIDA
     ANILKPALAR GELQCIGATT LDEYRKHIER DAALERRFQP VMVGEPSIED TIEILRGLRE
     RYEQHHRLRI TDEALEAAAT LGDRYISDRF LPDKAIDLID EAGSRVRLLN SKLPPEAKEV
     DKELRSVQKE KEDAVREQDF TRAGELRDKE VELRDKIRSL LQTSRQDIPA EQQASDENSG
     EPALATEGSE TSESAVTGTT PVVNEEDIAQ IVASWTGVPV QKLTESESVK LLNMEETLHK
     RLIGQDEAVK AVSKAIRRAR VGLKNPNRPI ASFIFSGPTG VGKTELTKAL AAYFFGSEDA
     MIRLDMSEFM ERHTVSKLIG SPPGYVGFNE GGQLTEAVRR RPYTVVLFDE IEKAHPDVFN
     LLLQLLEDGR LTDSKGRTVD FKNTLIIMTS NIGSKVIEKG GGGLGFEFSG ENAEENQYNR
     IRSLVNEELK QYFRPEFLNR LDEIIVFRQL NRDEVKEIAE IMLREVFGRI GEKGITLTVS
     DAFKERLVEE GYNPAYGARP LRRAVMRLLE DSLAEEVLTG RIKDGDEAEV DVEDGKVVVK
     HLNRTPSDIP ELASAGR
//
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