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Database: UniProt
Entry: A0A2V4A051_9BACT
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ID   A0A2V4A051_9BACT        Unreviewed;       832 AA.
AC   A0A2V4A051;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:PXY01956.1};
GN   ORFNames=DF185_04715 {ECO:0000313|EMBL:PXY01956.1};
OS   Marinifilum breve.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae.
OX   NCBI_TaxID=2184082 {ECO:0000313|EMBL:PXY01956.1, ECO:0000313|Proteomes:UP000248079};
RN   [1] {ECO:0000313|EMBL:PXY01956.1, ECO:0000313|Proteomes:UP000248079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC075 {ECO:0000313|EMBL:PXY01956.1,
RC   ECO:0000313|Proteomes:UP000248079};
RA   Fu T.;
RT   "Marinifilum breve JC075T sp. nov., a marine bacterium isolated from Yongle
RT   Blue Hole in the South China Sea.";
RL   Submitted (MAY-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:PXY01956.1}.
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DR   EMBL; QFLI01000002; PXY01956.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V4A051; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000248079; 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:PXY01956.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PXY01956.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          434..469
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          147..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          430..487
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   832 AA;  92816 MW;  4E8389EB277E53F1 CRC64;
     MDSKFSPRIK DVLSYSKEEA ERLGNSAIGT EHLFLGILRE GEGIAVDILI SLGVDLYDIR
     KNIEREIKSD TITDLDQNNI PLQRSAERVL KLIYLEAKAL KNNTIDTSHL LLAILKDDKS
     MVTQILEDQT VDYNKVKENL KTLFPKAQAD YPSEEREGKG GMSGGSKGSS ARGKSETPVL
     DNFGIDITKS AEEGTLDPIV GRETEIERLA QILSRRKKNN PILIGEPGVG KSAIAEGLAL
     RIVQKKVSRV LFGKRVVTLD LASIVAGTKY RGQFEERMKA ILNELSKTTD IILFIDEIHT
     IVGAGGATGS LDAANMLKPA LARGEIQCIG ATTLDEYRQN IEKDGALERR FQKVMVEPTS
     PEETIEILNN IKERYEDHHN VYYTDEAIDS CVKLTSRYIS DRYLPDKAID ALDEAGSRVH
     ISNIHVPVII EELEKKIEDT RQSKIKAVKA QKFELAASFR DKEKNFSEDL EKEKEKWEQE
     LSLKKEKVSE EDIAEVVAMM TGVPVKRIAQ AEGSRLLKMD DELQGKVVGQ DDAIAKIVKA
     IQRNRAGLKD PNKPIGTFIF LGPTGVGKTQ LAKVLSEYLF DSSDALIRID MSEYMEKFAV
     SRLVGAPPGY VGYEEGGQLT EKVRRKPYSV VLLDEIEKAH PDVFNILLQL LDDGQLTDSL
     GRRVDFKNSI IIMTSNIGSR ELKDFGKGIG FQTGGNDSNE YANSIIQKAL KKAFAPEFLN
     RIDDLIMFNS LTQKDIHKII DIELNGLYKR INDLGYNIKI STAAKDFIAE KGYDVQFGAR
     PLKRAIQKYL EDEMAEVIIK ASISEGDTIS VGLDKSKQKI TTKILKAQKE LE
//
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