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Database: UniProt
Entry: A0A1Z4J9Y8_LEPBY
LinkDB: A0A1Z4J9Y8_LEPBY
Original site: A0A1Z4J9Y8_LEPBY 
ID   A0A1Z4J9Y8_LEPBY        Unreviewed;       816 AA.
AC   A0A1Z4J9Y8;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=AAA ATPase {ECO:0000313|EMBL:BAY53576.1};
GN   ORFNames=NIES2135_03820 {ECO:0000313|EMBL:BAY53576.1};
OS   Leptolyngbya boryana NIES-2135.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Leptolyngbya.
OX   NCBI_TaxID=1973484 {ECO:0000313|EMBL:BAY53576.1, ECO:0000313|Proteomes:UP000217895};
RN   [1] {ECO:0000313|EMBL:BAY53576.1, ECO:0000313|Proteomes:UP000217895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2135 {ECO:0000313|EMBL:BAY53576.1,
RC   ECO:0000313|Proteomes:UP000217895};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-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}.
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DR   EMBL; AP018203; BAY53576.1; -; Genomic_DNA.
DR   RefSeq; WP_017291140.1; NZ_AP018203.1.
DR   AlphaFoldDB; A0A1Z4J9Y8; -.
DR   Proteomes; UP000217895; 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; -; 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   Reference proteome {ECO:0000313|Proteomes:UP000217895};
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          418..453
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
SQ   SEQUENCE   816 AA;  89657 MW;  E73B2CA4B9BC00D6 CRC64;
     MFEYFTDQAI ETIMFAQEEA RRLRQNSVGT EAVLLGLLRQ DDTIAVSVLH ELGADLSKVR
     SEVEKIVGYG NGASFGELPF TPKTRQILER ALQQAQMMGM RYVRAEHILL ALVDDNQGVA
     IKVLSQLGLN PAEIRAHITR AQAEPMAVGQ PTAPRKAAGS NKLVALNEFG TNLTQMAAEG
     KLDPMIGRQK ELDRVIQILG RRSKNNPVLV GEPGVGKTAI AEGLAQRIYD QAVPEILQDR
     QVFMLDMGGL LAGTRFRGEF EERMKQILDE VQQSGNVILF IDEIHTLVGA GSIGGGMDAA
     NLMKPALARG LLQCIGATTL DEYRQHIEQD AALERRFQPV MVGEPSVEET IDILRGLRDR
     YEQHHQLLID DAAVEAAAKL ADRYITDRFL PDKAIDLIDE AGSLVRLRHT NPALKALKKE
     LRQVQKEKQA TVAAQDFDKA GTLRDRELEL ERELSAGVPE AAMPTVTEED IAQVVASWTG
     VPVSKLTESE SAMLLHLDDV LHQRVIGQNE AVSAVARAIK RARVGLQSAD RPIASFIFSG
     PTGVGKTELA KALAVAVFGS EDAMIRLDMS EYMESHTVSK LIGSPPGYIG YDEGGQLTEA
     VRRNPYTVIL FDEVEKAHPD VFNLMLQLLD DGRLTDAKGR TVSFKNTLLI MTSNLGSKVI
     EKGGAGLGFA TETGSSDSVQ YNRIRTLVND ELKQYFRPEF LNRVDEIIVF RQLTRPEIIE
     IADLMIQEAA TRIAEQGISL EVSDRFKERV VVDGYNPSYG ARPLRRAIAR LLEDSLAEAF
     LAGQIQRGDT AIADVDDDQQ VVIKAVKMPV SIAASA
//
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