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Database: UniProt
Entry: A0A1V1ZFP9_9FLAO
LinkDB: A0A1V1ZFP9_9FLAO
Original site: A0A1V1ZFP9_9FLAO 
ID   A0A1V1ZFP9_9FLAO        Unreviewed;       849 AA.
AC   A0A1V1ZFP9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:OMP30955.1};
GN   ORFNames=BKM32_11370 {ECO:0000313|EMBL:OMP30955.1};
OS   Mangrovimonas sp. DI 80.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Mangrovimonas.
OX   NCBI_TaxID=1779330 {ECO:0000313|EMBL:OMP30955.1, ECO:0000313|Proteomes:UP000188854};
RN   [1] {ECO:0000313|EMBL:OMP30955.1, ECO:0000313|Proteomes:UP000188854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DI 80 {ECO:0000313|EMBL:OMP30955.1,
RC   ECO:0000313|Proteomes:UP000188854};
RA   Krishnamurthi S., Pal Y., Verma A., Sundharam S.;
RT   "Taxonomic characterization of strain DI 80 closely related to
RT   Mangrovimonas sp.";
RL   Submitted (DEC-2016) 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:OMP30955.1}.
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DR   EMBL; MSDT01000005; OMP30955.1; -; Genomic_DNA.
DR   RefSeq; WP_076664003.1; NZ_MSDT01000005.1.
DR   AlphaFoldDB; A0A1V1ZFP9; -.
DR   Proteomes; UP000188854; 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:OMP30955.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:OMP30955.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188854};
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          448..483
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          156..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          444..490
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        174..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   849 AA;  95484 MW;  B4CAFAE26507D27D CRC64;
     MDDNFSPRVK DVIAYSKEEA LRLGHDFIGT EHLMLGLLRN GSGKAIDILS ALDIDLNHLR
     RKVEILSPAN SNVATASNEK KNLHLTRQAE RALKTTFLEA KLFQSTSINT AHLLLCILRN
     ENDPTTKLLN KLKVDYDNVK EQFKFMITND DDFLESPKAE SYSDDDMADD DDSKQNPFGQ
     SSSKTTKKSK TPVLDNFGRD LTVLAEEGKL DPVVGREKEI QRVSQILSRR KKNNPLLIGE
     PGVGKSAIAE GLALRIVKRK VSRILFNKRV VTLDLASLVA GTKYRGQFEE RMKAVMNELE
     KNDDIILFID EIHTIVGAGG ATGSLDASNM FKPALARGEI QCIGATTLDE YRQYIEKDGA
     LERRFQKVIV EPTSVEETIE ILNNVKEKYE EHHNVDYTPE AIEACVKLTN RYMTDRFLPD
     KAIDALDEAG SRVHITNIEV PKQILELEKK LEEVRETKNT VVKKQKYEEA AKLRDDEKRL
     EKELAVAQEK WEEETKLHRE VVTEDNVADV VSMMTGIPVN RIAQTESNKL AKLPEHIKGK
     VIGQDEAVAK VVKAIQRNRA GLKDPNKPIG SFIFLGQTGV GKTQLAKVLA RELFDSEDAL
     IRIDMSEYME KFAISRLVGA PPGYVGYEEG GQLTEKVRRK PYAVILLDEI EKAHPDVFNM
     LLQVLDDGYL TDSLGRKIDF RNSIIIMTSN IGARKLKDFG QGVGFGTAAR EAQAHDNSKS
     IIENALKKAF APEFLNRIDD VIVFNALEKS DIDKIIDIEL AKLVERIKGL GYELKLSDKA
     KDYIADKGFD KQYGARPLKR AIQKYIEDAL AEEIINAQLQ EGDTIFMDLD SKTEELTIKI
     EKAEKHTES
//
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