ID Q2S2Z0_SALRD Unreviewed; 875 AA.
AC Q2S2Z0;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE SubName: Full=ATP-dependent Clp protease, ATPase subunit {ECO:0000313|EMBL:ABC45877.1};
GN Name=clpC {ECO:0000313|EMBL:ABC45877.1};
GN OrderedLocusNames=SRU_1317 {ECO:0000313|EMBL:ABC45877.1};
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC45877.1, ECO:0000313|Proteomes:UP000008674};
RN [1] {ECO:0000313|EMBL:ABC45877.1, ECO:0000313|Proteomes:UP000008674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31
RC {ECO:0000313|Proteomes:UP000008674};
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP000159; ABC45877.1; -; Genomic_DNA.
DR RefSeq; WP_011404069.1; NC_007677.1.
DR RefSeq; YP_445441.1; NC_007677.1.
DR AlphaFoldDB; Q2S2Z0; -.
DR STRING; 309807.SRU_1317; -.
DR EnsemblBacteria; ABC45877; ABC45877; SRU_1317.
DR GeneID; 83728232; -.
DR KEGG; sru:SRU_1317; -.
DR PATRIC; fig|309807.25.peg.1369; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_10; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000008674; Chromosome.
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:SF193; CHAPERONE PROTEIN CLPB; 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 Hydrolase {ECO:0000313|EMBL:ABC45877.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ABC45877.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008674};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 435..470
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 147..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 431..484
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 822..838
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 875 AA; 97251 MW; 62AC7EBEF7C14AE2 CRC64;
MEGNFSNRVR DVISYSREEA VRLGHDYIGT EHLLLGLIRE GDGIAVKILR NLGCDLLELK
EAVEDTVRST SSSTSVGNIP LTKQAEKVLK ITYLEAKLYK SDVIGTEHLL LSLLRDDENI
AAQILQQGFS VTYDAVRNEL DSIISGKASS SSSGSGGSGG RLSSGYGQES SESENSNTPV
LDNFGRDLTE LAEEDELDPI IGREEEIKRV AQILSRRKKN NPVLIGEPGV GKTAIAEGLA
ARIVDRKVSR VLYDKRIVTL DLASLVAGTK YRGQFEERMK AVMKELEDND DIILFIDEIH
TIVGAGGASG SLDASNMFKP ALARGDLQCI GATTLDEYRQ NIEGDGALDR RFQKIIVDPS
TPEETVNILS NIKSYYEDHH NVRFSEEAID LAVQLSDRYI TDRFLPDKAI DVMDEAGARV
HLSNIEVPPE ILELEEQIED VQEEKNQVVK SQRFEEAARL RDKEKTLQEE LEEAKQQWHE
QAETEVHDVT SEEIAEVVAM MTGIPVDKIS EPEQQKLLKM EESLKEHVVG QDEAIEKLSK
AIRRTRAGLK DPEKPIGSFI FLGPTGVGKT ELAKVLTEYL FDSQESLIRI DMSEYMEKFS
VSRLVGAPPG YVGHEEGGQL TEKVRRKPYS VVLLDEIEKA HPDVSNILLQ VLDDGILTDG
MGREVDFRNT ILIMTSNIGT QDIKSFGQGI GFDQTDGEDM DYTSMKSTVQ DALKNVFNPE
FLNRLDDVIV FNPLNKENIF DIIDIMSEDL FERAEELGLD LEFDEAAKEF LTDRGFDQKY
GARPLRRALQ KYVQDPMAED ILHDEITEGD TVLITHDGES EELSFEVEEG EAPTEETPTD
ENGEANSVSA EEVAEGASTD ENGSGEEPST ASDEE
//
