ID A0A0Q4C818_9SPHN Unreviewed; 790 AA.
AC A0A0Q4C818;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:KQM21832.1};
GN Name=clpA {ECO:0000313|EMBL:KQM21832.1};
GN ORFNames=ASE49_00470 {ECO:0000313|EMBL:KQM21832.1};
OS Novosphingobium sp. Leaf2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM21832.1, ECO:0000313|Proteomes:UP000050893};
RN [1] {ECO:0000313|EMBL:KQM21832.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM21832.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM21832.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM21832.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQM21832.1}.
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DR EMBL; LMJY01000001; KQM21832.1; -; Genomic_DNA.
DR RefSeq; WP_056767376.1; NZ_LMJY01000001.1.
DR AlphaFoldDB; A0A0Q4C818; -.
DR STRING; 1735670.ASE49_00470; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000050893; 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: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:KQM21832.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KQM21832.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050893};
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 REGION 144..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 86805 MW; 164F92693A1134C8 CRC64;
MPSFAQSLEK TLHSALSHAS ERSHEYATLE HLLLALIDDT DAAQVMQACG VDLGDLGDVV
RQYLDQEYQS LKTEEKGDPA PTAGFQRVIQ RAILHVQSSG KDTVTGANVL VALFSERDSY
AVYFLQQQDM SRLDAVSFIS HGIGKGGKRI EDRSPKGASD DAAPTPEDKA ETKAASNKKD
SALDQFTVNL NEKALKGKVD PLIGRGPEVD RTIQILCRRS KNNPLYVGDP GVGKTAIAEG
LARKIVEGDV PEVLAEAVIY SLDMGSLLAG TRYRGDFEER LKQVVSELEK MPHAVLFIDE
IHTVIGAGAT SGGAMDASNL LKPALSGGTI RCIGSTTYKE FRNHFEKDRA LLRRFQKIDV
NEPTVEDTIK ILKGLRTAFE EHHRVKYTPD AIKTAVELSA RYINDRKLPD KAIDVIDEVG
AMQMLVPPSR RKKTITSREI EQVIATMARI PPKSVSSDDK KALETLERDL KRVVFGQDKA
IALLSTAMKL SRAGLRDPDK PIGSFLFSGP TGVGKTEVAR QLASVMGIEL KRFDMSEYME
RHSISRLIGA PPGYVGFDQG GLLTDAIDQN PHCVLLLDEI EKAHPDLFNI LLQVMDNGRL
TDHHGKTVDF RNVVLIMTTN AGASDMARQG IGFGDTSKAD AGEEAVKQMF TPEFRNRLDA
IVPFAYLAKD TISRVVDKFI LQLELQLADQ NVHIQFDTDA RGWLGDRGYD KLYGARPMGR
VIQEKVKQPL AEELLFGKLA HGGEVHVSLK DDALNFELTP SAPRIGKARK KDAAKRAKKP
GIQPEPSAED
//
