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
//