ID A0A518DR67_9BACT Unreviewed; 1140 AA.
AC A0A518DR67;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:QDU94335.1};
GN Name=clpC_1 {ECO:0000313|EMBL:QDU94335.1};
GN ORFNames=Pla8534_21240 {ECO:0000313|EMBL:QDU94335.1};
OS Lignipirellula cremea.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Lignipirellula.
OX NCBI_TaxID=2528010 {ECO:0000313|EMBL:QDU94335.1, ECO:0000313|Proteomes:UP000317648};
RN [1] {ECO:0000313|EMBL:QDU94335.1, ECO:0000313|Proteomes:UP000317648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pla85_3_4 {ECO:0000313|EMBL:QDU94335.1,
RC ECO:0000313|Proteomes:UP000317648};
RA Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA Labrenz M., Spormann A.M., Op den Camp H., Overmann J., Amann R.,
RA Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT characterization uncovers novel biology.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP036433; QDU94335.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A518DR67; -.
DR KEGG; lcre:Pla8534_21240; -.
DR OrthoDB; 8857354at2; -.
DR Proteomes; UP000317648; 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; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 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; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR Pfam; PF07724; AAA_2; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:QDU94335.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:QDU94335.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:QDU94335.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000317648}.
FT DOMAIN 221..515
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 521..656
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 690..782
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 418..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 853..880
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 428..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1140 AA; 128545 MW; 64579E9A886E5860 CRC64;
MPLLPLRFDT VLCRYENDVR LHWPLFFREV SALGMKADRL EKAIRQGAVS VLRGEQTLQQ
SRRRAGVAPE LAVLQVSLSP PRRERSWSTP VELELGYLRW PHGAAWRAYV PALDIEIVAR
KEEELAALVA QQVQACMMRR GMVGSLQELT WLHRIREIST GSTEVETHVP SPRQVEQQAG
NAEPAKALLK AAERLDKNLP PEVFEVDDTV DRMGQLLTAH QPQSVLLVGP SGVGKSAVFG
QLVRRRQDCG LGRYAFWSTT GSRLVSGMTG FGMWQDRCRE IGDELRQQKA VLHLGNLLEL
MEVGKYEGND QGVADFFRPR LERGELLAVA ECTPEQLAMI ERKSPNLLQA FAQIRLEEPS
SPKMIAILQQ AAAQHPRSDR VRIAPEALEW IDRVHRRYAT YSARPGRPLR FLRNLLEDAP
APAEPPPNER TRAERKSDSA SRSAANRARL HQVELTQRDA MRAFSIETGL PLAMIDPQAP
LDLAALRTHF SNRLIGQTEA IDLIVDLIAV MKAGLTRPQR PIASLLFIGP TGVGKTEMAK
ALAEYLYHDA QRMTRIDMSE FSDPLAADRL LGGSFQGEGI LTAKVREQPF GVVLLDEFEK
AHPRLHDVLL QVLGEGRLTD AAGRLADFSN SVIIMTSNLG AESRRRLSLG FAEAGEPTQR
VREHFLAEVR RFVRPEFFNR IDRIVPFDSL SPAMITRIAQ RELAQLQQRD GVRFRPLQLK
LDDGLAERLA LQSYDPRYGA RPLKRAIERE LLAPLADQLN GHDDQTPLHA QAEWPATGRL
TVRVRPAPRD ADLTIMQQSA GDLADQFSQL RRQVQRLMRC AAVLQVRNQL FRLRREEKRW
RARNPQGPQI VKVQKELASL DEKKERIAAV RREIFGCEER LLMNCYTQQS LDLTQIRSQL
AQGKVAYEKQ LLELYGDLVD QQTHAGVVIY SEEPRWLGEL AAAYYAIAVR REMIVKLWTL
SALTDAQREA FLRSEDHHLA DGGELVGLGA SWTKEELALS KKTLLVATER TTVDADLFHK
MSLPTLGVFL GIHGPMAPLL WGEEQGVHQL VAGNKRQSCL VQAAHLMVEH LIPPDRIDRR
GTIVTKNPRR TYEKSRSTLH DRLLGQSFRW TSDDFSPPLE SLMMQAVLSQ AREKLGLAED
//