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
//