ID A0A0Q5TEG7_9BACT Unreviewed; 845 AA.
AC A0A0Q5TEG7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:KQS33647.1};
GN ORFNames=ASG33_06185 {ECO:0000313|EMBL:KQS33647.1};
OS Dyadobacter sp. Leaf189.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=1736295 {ECO:0000313|EMBL:KQS33647.1, ECO:0000313|Proteomes:UP000051810};
RN [1] {ECO:0000313|EMBL:KQS33647.1, ECO:0000313|Proteomes:UP000051810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS33647.1,
RC ECO:0000313|Proteomes:UP000051810};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS33647.1, ECO:0000313|Proteomes:UP000051810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS33647.1,
RC ECO:0000313|Proteomes:UP000051810};
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|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:KQS33647.1}.
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DR EMBL; LMPS01000001; KQS33647.1; -; Genomic_DNA.
DR RefSeq; WP_056281413.1; NZ_LMPS01000001.1.
DR AlphaFoldDB; A0A0Q5TEG7; -.
DR STRING; 1736295.ASG33_06185; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051810; 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; -; 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 Gene3D; 4.10.860.10; UVR domain; 1.
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; 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 InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 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.
DR PROSITE; PS50151; UVR; 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:KQS33647.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KQS33647.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051810};
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 DOMAIN 444..479
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 144..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 440..490
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 845 AA; 94435 MW; CEE6998B783EA8E4 CRC64;
MEAKFSNRVK EVISMSREEA LRLGHDYIGA EHLLLGMIRE GDGVAIGLLK KLGVSLDDVR
QTIEQATKGA ATNNVKNLQN IPLTRQSEKV LKITYLEAKI FKSTLIGTEH LLLSILRDED
NVGTQILHKF NVNYEVIKEM LEYQSSGSRP HMGPETEDGD DEARGGMFGG GGSSSGKESK
GAEKSRTPVL DNFGRDLTKM AEVGKLDPIV GREKEIERVA QILSRRKKNN PILIGEPGVG
KTAIAEGLAL RIVQKKVSRV LFGKRVVTLD LASLVAGTKY RGQFEERMKA VMNELEKSPD
VILFIDELHT IVGAGGASGS LDASNMFKPA LSRGEIQCIG ATTLDEYRQY IEKDGALARR
FQMVMVDATS IEETIQILEN IKDKYEDHHH VNYTPESIST AVKLSERYIT DRFLPDKAID
VLDEVGARVH ISNITVPEDI LLLEEQIENI KQEKNRVVKS QKYEEAAQLR DREKKLIDQL
DRAKLAWEEE TKQKRYTVTE QNVAEVVAMM TGIPVTNVSM DEGKKLLNMA DELKGKVIGQ
DPPIEKLVKA IQRTRVGLKD PKKPIGSFIF LGPTGVGKTE LAKVLSTYLF DKDDSLVRID
MSEYMEKFSV SRLVGAPPGY VGYEEGGQLT EKIRRKPYSV VLLDEIEKAH PDVFNILLQV
LDDGILTDGL GRRVDFRNTI IIMTSNIGAR DLKDFGTGIG FSTKAKSENQ DEIMKGTIQS
ALRKAFSPEF LNRLDDVIVF NSLQREDLHR IIDISLGKLF SRVKGLGYEI ELTIPAKDFL
SEKGYDPQYG ARPLNRAIQK YLEDPVAEEI LKGDLREGDV LVANHEENSE QLVITVRKKE
EELAN
//