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
//