ID L8LWF8_9CYAN Unreviewed; 822 AA.
AC L8LWF8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=ATPase with chaperone activity, ATP-binding subunit {ECO:0000313|EMBL:ELS00342.1};
GN ORFNames=Xen7305DRAFT_00000420 {ECO:0000313|EMBL:ELS00342.1};
OS Xenococcus sp. PCC 7305.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC Xenococcus.
OX NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS00342.1, ECO:0000313|Proteomes:UP000011203};
RN [1] {ECO:0000313|EMBL:ELS00342.1, ECO:0000313|Proteomes:UP000011203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS00342.1,
RC ECO:0000313|Proteomes:UP000011203};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {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:ELS00342.1}.
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DR EMBL; ALVZ01000234; ELS00342.1; -; Genomic_DNA.
DR RefSeq; WP_006512495.1; NZ_ALVZ01000234.1.
DR AlphaFoldDB; L8LWF8; -.
DR STRING; 102125.Xen7305DRAFT_00000420; -.
DR PATRIC; fig|102125.3.peg.5417; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000011203; 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; -; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000011203};
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 417..452
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
SQ SEQUENCE 822 AA; 91483 MW; 1AB5BD3AC2481C4A CRC64;
MFERFTEKAI KVIMLAQEEA RRLGHNFVGT EQILLGLIGE GTGVAAKVLK SMGVNLKDAR
IEVEKIIGRG SGFVAVEIPF TPRAKRVLEL SLEEARQLGH NYIGTEHLLL GLIREGEGVA
ARVLENLGVD LSKVRTQIIR MLGETAEVAT GGGSSGRNKT PTLDEFGSNL TQMASEGKLD
PVVGRQKEIE RVIQILGRRT KNNPVLIGEP GVGKTAIAEG LAQRIANQDI PDILEEKRVV
TLDIGLLVAG TKYRGEFEER LKKIMDEIRQ AGNVILVIDE VHTLIGAGAA EGAIDAANIL
KPALARGELQ CIGATTLDEY RKHIERDAAL ERRFQPVMVG EPSVEETIEI LYGLRERYEQ
HHKLKILDEA LEAAAKLSDR YISDRYLPDK AIDLIDEAGS RVRLINSQLP PAAKELDKEL
RGILKEKDDA VRSQDFDKAG SLRDREMEIK EQIRNIASAK KSEEDTETNS PFVDSEEIAH
IVASWTGVPV NKLTETESEK LLHMEDTLHQ RIIGQEDAVK AISRAIRRAR VGLKNPNRPI
ASFVFSGPTG VGKTELTKAL ATYFFGSEEA MIRLDMSEYM ERHTVSKLIG SPPGYVGYNE
GGQLTEAVRR RPYTVVLFDE IEKAHPDIFN MLLQILEDGR LTDAKGRTVD FKNTLLILTS
NIGSKVIEKG GGGLGFEFED NAGEAQYNRI KSLVNEELKN YFRPEFLNRL DEIIVFRQLS
KDEVKEIAEI LLKEVFTRLT EKEIDLEVTD KFKERLVDEG FNPAYGARPL RRAIMRLLED
VLAEEILSGR LGEGDTAVVD VNEEGKVKIL PQLKKKELLP SS
//
