ID K9V5F2_9CYAN Unreviewed; 817 AA.
AC K9V5F2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=ATPase AAA-2 domain protein {ECO:0000313|EMBL:AFZ03031.1};
GN ORFNames=Cal6303_4117 {ECO:0000313|EMBL:AFZ03031.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ03031.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFZ03031.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ03031.1,
RC ECO:0000313|Proteomes:UP000010477};
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., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
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; CP003610; AFZ03031.1; -; Genomic_DNA.
DR RefSeq; WP_015199655.1; NC_019751.1.
DR AlphaFoldDB; K9V5F2; -.
DR STRING; 1170562.Cal6303_4117; -.
DR KEGG; calt:Cal6303_4117; -.
DR PATRIC; fig|1170562.3.peg.4488; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_3; -.
DR OrthoDB; 438311at2; -.
DR Proteomes; UP000010477; 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:UP000010477};
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 420..455
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT COILED 409..436
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 817 AA; 90305 MW; 8E35AECA1F0E1973 CRC64;
MFEHFTSQAI RVIMLAQEEA RRLGHNFVGT EQILLGLIGE GNGVAAKVLV DLGVTLKDAR
REVEKIIGRG SGFVPPEIPF TPKVKSLFEQ AFKEARSLGN NYISTEHLLL GLTEAGEGVA
AKVLQNLGID LSEVRTAVIR RLGDDVAVAP GAGASSGGQR RNQQSLMLEE FGKNLTKLAQ
EGKLDPVVGR ANEIERAVQI LGRRTKNNPV LIGEPGVGKT AIAEGLAQRI VNQDVPEILL
GKQVVSLDMG LMVAGTRFRG DFEERLKKVM EEIRTEGNII LVIDEIHTLV GAGGVEGGMD
AANIMKPALA RGELQCLGAT TLNEYRNIER DAALERRFQP ILVGEPSVEE TIHILQGLRS
VYEQHHRVTI TDEALQAAAE LSDRYISDRF LPDKAIDLID EAGSRVRLRN SQISQSRELK
RQLRSLSKEK DEAVRVQDFE KAGQLRDKEI ELEGQIQAES SDYNNNPIVN EEDIAQIVAS
WTGVPVNKLT ESESEMLMHL EDTLHQRLIG QEQAVTAVSR AVRRARVGLK NPNRPIASFI
FSGPTGVGKT ELAKSLAAYF FGAEDAMIRL DMSEFMERHT VSKLIGSPPG YVGYEEGGQL
TEAVRRKPYT VILFDEIEKA HPDVFNMLLQ LLDDGHLTDA KGRKVDFKNT LIILTSNIGS
KVIEKGGGGI GFQFDDASEA SYNRIKTLVN EELKNFFRPE FLNRLDDIIV FTQLNKDEVK
QIAEIMLLDV GSRLKERGII LQVSDRFKER VVQEGYDPSY GARPLRRAIM RLLEDSLAEA
MLSGQIVDGD TALIDVDDDG KVKVIKSESR ELLLASI
//
