ID A0A265UTH9_9FLAO Unreviewed; 851 AA.
AC A0A265UTH9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:OZV68623.1};
GN ORFNames=CA834_09155 {ECO:0000313|EMBL:OZV68623.1};
OS Winogradskyella aurantia.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=1915063 {ECO:0000313|EMBL:OZV68623.1, ECO:0000313|Proteomes:UP000216840};
RN [1] {ECO:0000313|EMBL:OZV68623.1, ECO:0000313|Proteomes:UP000216840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WNB302 {ECO:0000313|EMBL:OZV68623.1,
RC ECO:0000313|Proteomes:UP000216840};
RA Sun Y., Chen B., Du Z.;
RT "The draft genome sequence of Idiomarina salinarum WNB302.";
RL Submitted (MAY-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:OZV68623.1}.
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DR EMBL; NGJN01000004; OZV68623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A265UTH9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000216840; 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:OZV68623.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:OZV68623.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216840};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 450..485
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 150..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 446..499
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 177..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 95473 MW; 3DD194450BD3344E CRC64;
MDDNFSPRVK DVIAFSKEEA LRLGHDFIGT EHLMLGLLRD GNGKAIDILS ALDVDLNHLR
RKVEILSPAN PNIVASSNEK KNLHLTRQAE RALKTTFLEA KLFQSTSINT AHLLLCILRN
ENDPTTKLLN KLKVDYDNVK EEFKSMITSE DDYLDTPKSE SYSDDDINEE EDDAKQNPFG
SGSSSKTNKK SKTPVLDNFG RDLTVLAEEG KLDPVVGREK EIQRVSQILS RRKKNNPLLI
GEPGVGKSAI AEGLALRIVK RKVSRTLFNK RVVTLDLASL VAGTKYRGQF EERMKAVMNE
LEKNDDIILF IDEIHTIVGA GGATGSLDAS NMFKPALARG EIQCIGATTL DEYRQYIEKD
GALERRFQKV IVEPTTVEET VEILNNIKGK YEEHHNVDYT DEAIEACVKL TNRYMTERFL
PDKAIDALDE AGSRVHITNI DVPEQILELE KKLEAVKETK NSVVKKQKYE EAAKLRDDEK
RLEKELLSAQ QKWEEETKQH REIVTEDNVA DVVSMMTGIP VNKIAQTEIN KLAKLSELIT
GKVIGQDQAV AKVVKAIQRN RAGLKDPNKP IGSFIFLGQT GVGKTQLAKI LAKELFDSDD
ALVRIDMSEY MEKFAISRLI GAPPGYIGYE EGGQLTEKIR RKPYAVVLLD EIEKAHPDVF
NMLLQVLDDG YLTDSLGRKI DFRNTIIIMT SNIGARKLKD FGTGVGFGTS AKAAQEADYA
KGVIENALKK AFAPEFLNRI DDVVVFNTLE KEDINKIIDI ELVKLIDRIK DLGYTLKLTD
KAKDYIAEKG FDKQYGARPL KRAIQKYVED TLAEEIINSK IQEGDTITMD FDSKNDELKI
KVKSSSKTTE S
//
