ID A0A261Q0W7_9BACT Unreviewed; 841 AA.
AC A0A261Q0W7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:OZI06027.1};
GN ORFNames=BWI93_22360 {ECO:0000313|EMBL:OZI06027.1};
OS Siphonobacter sp. BAB-5385.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Siphonobacter.
OX NCBI_TaxID=1864822 {ECO:0000313|EMBL:OZI06027.1, ECO:0000313|Proteomes:UP000215802};
RN [1] {ECO:0000313|EMBL:OZI06027.1, ECO:0000313|Proteomes:UP000215802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-5385 {ECO:0000313|EMBL:OZI06027.1,
RC ECO:0000313|Proteomes:UP000215802};
RA Dhebar S., Dhebar S., Bhargava P., Bagatharia S.B., Soni S., Joshi M.N.;
RT "Draft genome of Siphonobacter sp. BAB-5385.";
RL Submitted (JUN-2017) 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:OZI06027.1}.
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DR EMBL; NMPS01000214; OZI06027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261Q0W7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000215802; 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:SF193; CHAPERONE PROTEIN CLPB; 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:OZI06027.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:OZI06027.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000215802};
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 440..475
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 147..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 436..486
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 841 AA; 94100 MW; 7D86223B7F751DAA CRC64;
MEAKFSNRVK EVISLSREEA LRLGHDYIGT EHLLLGMIRE GEGVAVALLK KLSINLDELR
MTIEQATKGT ATHSVRNMAN IPLTRQSEKV LKMTHLEAKV FKTQLIGTEH VLLAILRDED
NIATQILHKF NVNYEIVKEM LEYQSNPNIN AGPDTDDNDE DSRMFGSSPR SESGKPGAEK
SRTPVLDNFG RDLTKLAELG KLDPIVGREK EIERVAQILS RRKKNNPILI GEPGVGKTAI
AEGLALRIVQ KKVSRVLFGK RVVTLDLASL VAGTKYRGQF EERMKAVMNE LEKSPEVILF
IDEIHTIVGA GGASGSLDAS NMFKPALARG DIQCIGATTL DEYRQYIEKD GALARRFQMV
MVDATSIEET VEILNNIKDK YEDHHHVNYT PEALEAAVKL SERYISDRFL PDKAIDVLDE
VGARVHINNI SVPEDIIQLE EAVEEVKKQK NQVVKSQKYE EAAQLRDREK KLLEQLDRAK
QRWEEDTKTR RYTVTEDNVA EVVAMMTGIP VRSVSTDEGK KLLTLAEDLK GKVIGQESAI
EKLAKAIQRT RVGLKDPKKP IGSFIFLGPT GVGKTELAKV LASHLFDKDD SLVRIDMSEY
MEKFSVSRLV GAPPGYVGYE EGGQLTEKIR RKPYSVVLLD EIEKAHPDVF NILLQVLDDG
ILTDGLGRRV DFRNTIIIMT SNIGARDLKD FGTGIGFATK TRVEGQDEAV KSTIQNALRK
AFSPEFLNRL DDVIVFNSLE REHLHRIIEL MLGKLFARIT TLGYRVELTE AAKDFLAKKG
YDPQYGARPL NRAIQRYLED PVAEEILKGD LAEGDILLAD HDGTSETLTI TAKKPETITE
E
//
