ID F3BY46_PSESG Unreviewed; 853 AA.
AC F3BY46;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:EGH06096.1};
DE Flags: Fragment;
GN ORFNames=Pgy4_00120 {ECO:0000313|EMBL:EGH06096.1};
OS Pseudomonas savastanoi pv. glycinea str. race 4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=875330 {ECO:0000313|EMBL:EGH06096.1, ECO:0000313|Proteomes:UP000005466};
RN [1] {ECO:0000313|EMBL:EGH06096.1, ECO:0000313|Proteomes:UP000005466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000005466};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGH06096.1}.
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DR EMBL; ADWY01000004; EGH06096.1; -; Genomic_DNA.
DR AlphaFoldDB; F3BY46; -.
DR PATRIC; fig|875330.6.peg.21; -.
DR HOGENOM; CLU_334513_0_0_6; -.
DR Proteomes; UP000005466; Unassembled WGS sequence.
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; -; 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; IPR017729; ATPase_T6SS_ClpV1.
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 NCBIfam; TIGR03345; VI_ClpV1; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF184; ATPASE WITH CHAPERONE ACTIVITY-RELATED; 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.
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:EGH06096.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EGH06096.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..134
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 142..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 420..471
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 149..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGH06096.1"
SQ SEQUENCE 853 AA; 93765 MW; E6452934761AA444 CRC64;
RTATESAAAL CLSENHYDVE VEHLLLQLLD NNDNDLPVIL RHYDVVPDRL QAQLVTALGT
FKKGNTRTPA LSPHITRMIE QAWVLASIEF GQSQIRTGHL IQALLDDDAL RRVVIGSAPE
LEKINADDLR LNMSALVEGS PETKLSKPLA NADASTDATT KGNGKTPALD QYTINLTQSA
RDGRIDPVLG REFEVRQMVD ILTRRRQNNP ILTGEAGVGK TAVVEGLALR IVQGDVPSVL
KGVAIHTLDL GLLQAGAGVK GEFENRLKSV IEETKRSLHP IILFIDEAHT LIGSGGQAGQ
NDAANLLKPA LARGELRTIA ATTWAEYKKY FEKDAALARR FQVVKVEEPD EDKAIHMLRG
LLAKMQEHHK VTVMDEALVQ AVRLSNRYIT GRQLPDKAVS VLDTACARVA LGQSAQPGAL
EDCKRHIDNL NAEITVLEQE TAKGSDHARR LTALHEELKA EQETRESLEQ QWKRELELVE
KLGALSVPED GAPDAEQIAA VRAELASVQG EQPLVHALVD GGTIGEVISG WTGIPLGKML
RDEIDTVQSL PALLGERVLG QDHALEEIGK RIKISRARME DPNKPIGVFL LLGPSGVGKT
ETALALADTL YGGERNVITI NMSEYQEAHT VSSLKGSPPG YVGYGEGGVL TEAVRRKPYS
VVLLDEVEKA HPDVLELFFQ VFDKGVLDDG EGREINFRNT VIILTSNTGT DRIMQWCLNT
EQKPTPDDIV EGLRDELNQV FKPAFLGRLT IVPYYPVQDA ILERIVGLKL ERIRKRFERN
HQAVLRYDEA LIKAIASRCT EVDSGARNID NILSKTLMPE LAQRVLERMA QDKPIQSLTI
DLGSDGDFAY TLT
//
