ID B5ZN72_RHILW Unreviewed; 830 AA.
AC B5ZN72;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 108.
DE SubName: Full=ATP-dependent Clp protease, ATP-binding subunit clpA {ECO:0000313|EMBL:ACI54862.1};
GN OrderedLocusNames=Rleg2_1572 {ECO:0000313|EMBL:ACI54862.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI54862.1, ECO:0000313|Proteomes:UP000008330};
RN [1] {ECO:0000313|EMBL:ACI54862.1, ECO:0000313|Proteomes:UP000008330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304 {ECO:0000313|EMBL:ACI54862.1,
RC ECO:0000313|Proteomes:UP000008330};
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(2010).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP001191; ACI54862.1; -; Genomic_DNA.
DR RefSeq; WP_012557540.1; NC_011369.1.
DR AlphaFoldDB; B5ZN72; -.
DR STRING; 395492.Rleg2_1572; -.
DR KEGG; rlt:Rleg2_1572; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_5; -.
DR OMA; GRVIQEH; -.
DR Proteomes; UP000008330; 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:0043335; P:protein unfolding; IEA:InterPro.
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 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; IPR013461; ClpA.
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 NCBIfam; TIGR02639; ClpA; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 1.
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 Hydrolase {ECO:0000313|EMBL:ACI54862.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ACI54862.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 144..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..799
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 90791 MW; 752AD51516CC9DE0 CRC64;
MPTFSPSLEK ALHQALTFAN ERHHEYATLE HLLLALIDDA DAAAVMGACN VDLDALRKTL
VEYVDNELSN LITGYDEDSK PTSGFQRVIQ RAVIHVQSSG REEVTGANVL VAIFAERESH
AAYFLQEQEM TRYDAVNYIS HGIGKRPGAS EARPPRGAEE EAESSKPTAR GGEEEGGPKK
QQDALKAYCV NLNEKAKGGK IDPLIGRHAE VSRTIQILCR RSKNNPLYVG DPGVGKTAIA
EGLAKRIVEG KVPEALADAT IFSLDMGTLL AGTRYRGDFE ERLKQVVKEL EEYPGAVLFI
DEIHTVIGAG ATSGGAMDAS NLLKPALSSG AIRCIGSTTY KEYRQFFEKD RALVRRFQKI
DVSEPSIDDA IEIMKGLKPY FEEYHHLRYS NDAIKSAVEL SARYISDRKL PDKAIDVIDE
TGAAQMLLPP SKRRKLITEK EIEATVATMA RIPPKTVSKD DEAVLANLEQ ELRSVVYGQD
IAIEALSTSI KLARAGLREP NKPIGAYVFS GPTGVGKTEV AKQLASSLGV ELLRFDMSEY
MERHTVSRLL GAPPGYVGFD QGGLLTDGVD QHPHCVVLLD EIEKAHPDIY NILLQVMDHG
TLTDHNGKKI DFRNVILIMT TNAGASEMAK AAIGFGSSKR TGEDEEALTR LFTPEFRNRL
DAIIPFAALP TAVIHKVVQK FIMQLEAQLS ERNVTFDLHE DAIAWLSEKG YDEKMGARPL
ARVIQDTIKK PLANEILFGK LKKGGVVNVT VGPKEDGKPG IVLEAIPDTA PIKPKPEAEV
VHPDADDQGD GELKTKAAPK TRAKTVPQAE PEVRDAPKKG STVPKVPRKK
//