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Database: UniProt
Entry: A0A1Z4RRR8_9CHRO
LinkDB: A0A1Z4RRR8_9CHRO
Original site: A0A1Z4RRR8_9CHRO 
ID   A0A1Z4RRR8_9CHRO        Unreviewed;       823 AA.
AC   A0A1Z4RRR8;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=ATP-dependent Clp protease ATPase subunit {ECO:0000313|EMBL:BAZ45138.1};
GN   ORFNames=NIES4102_21560 {ECO:0000313|EMBL:BAZ45138.1};
OS   Chondrocystis sp. NIES-4102.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Chondrocystis.
OX   NCBI_TaxID=2005460 {ECO:0000313|EMBL:BAZ45138.1, ECO:0000313|Proteomes:UP000217698};
RN   [1] {ECO:0000313|EMBL:BAZ45138.1, ECO:0000313|Proteomes:UP000217698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-4102 {ECO:0000313|EMBL:BAZ45138.1,
RC   ECO:0000313|Proteomes:UP000217698};
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; AP018281; BAZ45138.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z4RRR8; -.
DR   KEGG; chon:NIES4102_21560; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000217698; 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   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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|ARBA:ARBA00023054};
KW   Hydrolase {ECO:0000313|EMBL:BAZ45138.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:BAZ45138.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217698};
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"
FT   REGION          455..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   823 AA;  91638 MW;  2FA660DB2C34E866 CRC64;
     MFERFTEKAI KVIMLAQEEA RRLGHNFVGT EQILLGLIGE GTGVAAKVLK SMGVNLKDAR
     IEVEKIIGRG SGFVAVEIPF TPRAKRVLEL SLEEARQLGH NYIGTEHLLL GLIREGEGVA
     ARVLENLGVD LSKVRTQVIR MLGETAEVAA GSSGTQGRNK TPTLDEFGSN LTQMAGEGKL
     DPVVGRQKEI ERVIQILGRR TKNNPVLIGE PGVGKTAIAE GLAQRIANKD IPDILEDKRV
     VTLDIGLLVA GTKYRGEFEE RLKKIMDEIR QAGNVILVID EVHTLIGAGA AEGAIDAANI
     LKPALARGEL QCIGATTLDE YRKHIERDAA LERRFQPVQV GEPSVDETIE ILYGLRERYE
     QHHKLKILDE ALEAAAKLSD RYISDRFLPD KAIDLIDEAG SRVRLINSQL PPAAKELDKE
     LREILKQKDD AVRSQDFDQA GELRDREMEI KEQIRNIAST KKNESDTGED SPVVDSEEIA
     HIVASWTGVP VNKITESESE KLMHMEDTLH QRIIGQEDAV KAISRAIRRA RVGLKNPNRP
     IASFIFSGPT GVGKTELTKA LATYFFGSED AMIRLDMSEY MERHTVSKLI GSPPGYVGYN
     EGGQLTEAVR RRPYTVVLFD EIEKAHPDIF NMLLQILEDG RLTDAKGRTV DFKNTLLILT
     SNIGSKVIEK GGGGLGFEFA DDQAEAKYNR IRSLVNEELK SYFRPEFLNR LDEIIVFRQL
     NKDEVKEISE ILLKEVFQRL TEQEISLEVT DKFKDRLVDE GYNPAYGARP LRRAIMRLLE
     DVLAEEILSG RLGEGDTAVV DIDEENKVTV VPQKEKVELL PSS
//
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