ID A0A2T7BP94_9BACT Unreviewed; 840 AA.
AC A0A2T7BP94;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:PUZ29494.1};
GN ORFNames=DCC81_08605 {ECO:0000313|EMBL:PUZ29494.1};
OS Chitinophaga parva.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2169414 {ECO:0000313|EMBL:PUZ29494.1, ECO:0000313|Proteomes:UP000244450};
RN [1] {ECO:0000313|EMBL:PUZ29494.1, ECO:0000313|Proteomes:UP000244450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY-1 {ECO:0000313|EMBL:PUZ29494.1,
RC ECO:0000313|Proteomes:UP000244450};
RA Chen K.;
RT "Chitinophaga fuyangensis sp. nov., isolated from soil in a chemical
RT factory.";
RL Submitted (APR-2018) 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:PUZ29494.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QCYK01000001; PUZ29494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7BP94; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000244450; 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:PUZ29494.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PUZ29494.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244450};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 438..473
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 148..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 434..484
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 840 AA; 94626 MW; DAFF6DD1DDB1D760 CRC64;
MDQNFSPQVK EIISFSREEA LRLGNDFIGT EHLLLGIIRE GEGTAVKILQ ALNVDLYELR
KEVELAVKDK TGKNIANINS LPLTKQAEKV IRVTVLEAKA LKSPTVETEH LMLSILKNKE
NVCTQILQQF DVDYDTFKNE LGFVKSSEPK AEFDDPGEEE FEDERKSYSS KAKQANTKSK
TPVLDNFGRD ITKLAESGSL DPIVGREQEI ERVSQILSRR KKNNPILIGE PGVGKTAIVE
GLALRIVQRK VSRVLFDKRV VSLDLAALVA GTKYRGQFEE RMKAIMNELE KNRDVILFID
EIHTIVGAGG ASGSLDASNI FKPALARGEL QCIGASTLDE YRMYIEKDGA LDRRFQKVMV
DPPTVDETIQ ILNNIKPRYE EYHNVSYNQE AIDACVKLSD RYMTDRLLPD KAIDVLDEVG
ARVHLKNINV PQNILDLEKQ IEDIKQEKNK VVKSQRFEEA AALRDTEKKL GEDLEKAKAN
WEEEVKHKRY PIDEEAIAEV VSMMTGIPVK RMVQAETEKL RRMGEDLKGA VVGQDDAIVK
VTKAIQRNRV GLKDPKKPIG TFIFLGPTGV GKTELAKSLA RYMFDSEDAL IRIDMSEYME
KFSVSRLIGA PPGYVGYEEG GQLTEKVRRK PYSVILLDEI EKAHPDIYNL LLQVLDDGIL
TDGLGRKVDF KNTLIIMTSN IGARQLKDFG AGVGFSTNNR IANEEENTKA VIEKALKRTF
SPEFLNRIDD VIIFNSLSKE HIYTIIDITM QSVLKRLNNL GFSLELTDEA KGFLADKGYD
QQFGARPLHR AIQKYLEDPL AEEILNMNIH NGDVLIADLD KENQKLVFTI KKQGSEVTQI
//
