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Database: UniProt
Entry: A0A401IG01_APHSA
LinkDB: A0A401IG01_APHSA
Original site: A0A401IG01_APHSA 
ID   A0A401IG01_APHSA        Unreviewed;       790 AA.
AC   A0A401IG01;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=ATPase AAA-2 domain protein {ECO:0000313|EMBL:GBF80141.1};
GN   ORFNames=AsFPU1_1542 {ECO:0000313|EMBL:GBF80141.1};
OS   Aphanothece sacrum FPU1.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Aphanothece.
OX   NCBI_TaxID=1920663 {ECO:0000313|EMBL:GBF80141.1, ECO:0000313|Proteomes:UP000287247};
RN   [1] {ECO:0000313|Proteomes:UP000287247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FPU1 {ECO:0000313|Proteomes:UP000287247};
RA   Kanesaki Y., Yoshikawa S., Ohki K.;
RT   "Physiological properties and genetic analysis related to exopolysaccharide
RT   production of fresh-water unicellular cyanobacterium Aphanothece sacrum,
RT   Suizenji Nori, that has been cultured as a food source in Japan.";
RL   Submitted (MAY-2017) 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:GBF80141.1}.
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DR   EMBL; BDQK01000006; GBF80141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401IG01; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000287247; 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   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.
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   Reference proteome {ECO:0000313|Proteomes:UP000287247};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
SQ   SEQUENCE   790 AA;  87836 MW;  D485AA0326B7BABA CRC64;
     MFEYFTDKAI KAIMLAQEEA RRTGQNLVGT EHLLLGLIGE GTGISAKVLG EFGLTLAQTR
     HIIQKITKKG VGFSPANIPF TSMVKLILER AFQEARQQGD RYVTTEHILL VLICDPDAVA
     VKAIKLQNID LAELRTTLID RIEEQEPVPV AAFDEPIGFE RPSGKKTRLE DFGVNLTQKA
     REGKLDPVVG RTKEIERTIQ ILGRRTKNNP VLVGEPGVGK TAIAEGLAQR IVAGEIPELL
     INKEVMTLDM GLLVAGTRFR GDFEERLKAI VEEVKKAGNI ILVIDEVHTL VGAGNMGGGM
     DAANLLKPAL ARGELQCLGT TTLDEYRQYI ERDGALERRF QCVMVGEPSV SETIEILLGL
     RKEYEAYHKV KFDDQALESA AKLADRYISD RFLPDKAIDL MDEAGSRTHL RHSLQTKMAS
     SVEGQNSSVI INPDSLIPVV DEEEIAHIVA AWTGIPVNKL TETESESLLY LEDHLHERII
     GQSEAVKAIS RSLRRARVGL KNPHRPIASF IFAGPTGVGK TELTKALAKY LFGSDDSMIR
     LDMSEYMESH TISKLIGSPP GFMGYEDGGQ LTEAVRRHPY GVVLFDEIEK AHPDVFNLLL
     QVLEDGRLTD AKGRTVDFNN TLIIMTSNIG SKVIEKGGNG FGFETDSNQD NAQYKRLQEL
     VNNELKQYFR PEFLNRLDEI IVFHQLNKSE VTKIADILLQ EVAKQLQEQR QMTLTVTDKF
     KELVVNEGYD PSYGARPLRR AIMRRLEDSL VEAILLGQVK DGEQLKVDVN EQNQVIVKSV
     KKLALSSVIG
//
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