ID J7QIS4_METSZ Unreviewed; 811 AA.
AC J7QIS4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=ATP-dependent Clp protease, ATP-binding subunit ClpA {ECO:0000313|EMBL:CCJ08601.1};
GN OrderedLocusNames=BN69_3150 {ECO:0000313|EMBL:CCJ08601.1};
OS Methylocystis sp. (strain SC2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylocystaceae; Methylocystis.
OX NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ08601.1, ECO:0000313|Proteomes:UP000005263};
RN [1] {ECO:0000313|EMBL:CCJ08601.1, ECO:0000313|Proteomes:UP000005263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:CCJ08601.1,
RC ECO:0000313|Proteomes:UP000005263};
RX PubMed=23045511; DOI=10.1128/JB.01446-12;
RA Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT Methanotroph with High-Affinity Methane Oxidation Potential.";
RL J. Bacteriol. 194:6008-6009(2012).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; HE956757; CCJ08601.1; -; Genomic_DNA.
DR RefSeq; WP_014892627.1; NC_018485.1.
DR AlphaFoldDB; J7QIS4; -.
DR STRING; 187303.BN69_3150; -.
DR KEGG; msc:BN69_3150; -.
DR PATRIC; fig|187303.17.peg.3410; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_5; -.
DR OMA; GRVIQEH; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000005263; 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:CCJ08601.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CCJ08601.1};
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 147..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 811 AA; 89862 MW; 5C28893B9A1A90C2 CRC64;
MPTFSRNLKQ TLDRALASAR ERRHEYATLE HLLLSLVEDV DASAVLRACS VDLDVLTKNL
RDYIDRELDN LVNEDADECK PTAGFQRVVQ RAIISVQSSG REDVSGANVL VALFAERESH
AVYFLQEQDM TRYDAVNFIS HGIAKRPGLS DASRSPRGVE EDGERSEGRE GRDGESRKKE
GALEAYCVNL NRKARDGRID PLIGREPEVL RTIQVLCRRQ KNNPLLVGDP GVGKTAIAEG
LARKIVSNEV PEVLAGATVF ALDMGALLAG TRYRGDFEER LKQVVKEIEN HKNAILFIDE
IHTVIGAGAT SGGAMDASNL LKPALAQGVL RCIGSTTYKE YRQYFEKDRA LVRRFQKIDV
NEPSIPDAIE IVKGLKPYFE EFHKIRYTND ALKAAVELSA RYIHDRKLPD KAIDVIDETG
AAQMLVAENK RKKTIGLKEI ETTIATMARV PPKTVSKDDA EVLAHLDETL RRVVYGQDKA
ISALTSAIKL ARAGLRDQEK PIGCYLFSGP TGVGKTEAAR QLATSLGIEL VRFDMSEYME
RHTVSRLIGA PPGYVGFDQG GLLTDAIDQH PHCVLLLDEI EKAHPDLYNI LLQVMDHGKL
TDHNGKTIDF RNVILIMTTN AGAQDLARTP IGFTRTRRDL DDSEAINRLF APEFRNRLDA
IVPFGHLPVD VIKRVVDKFI MQLEAQLADR NVTIELTDEA RSWLVEHGYD ESMGARPMSR
VIHQHIKTPL ADEVLFGRLK NGGAVRVVVV GDDSGAKSLG FVFPEGPVLP RPERDIFEAG
KKRAAEEAAS GDDAIRAADT ERDERPAPLK S
//