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Database: UniProt
Entry: A0A0X8G4A9_9FLAO
LinkDB: A0A0X8G4A9_9FLAO
Original site: A0A0X8G4A9_9FLAO 
ID   A0A0X8G4A9_9FLAO        Unreviewed;       844 AA.
AC   A0A0X8G4A9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:AMC09785.1};
GN   ORFNames=Lupro_00235 {ECO:0000313|EMBL:AMC09785.1};
OS   Lutibacter profundi.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lutibacter.
OX   NCBI_TaxID=1622118 {ECO:0000313|EMBL:AMC09785.1, ECO:0000313|Proteomes:UP000059672};
RN   [1] {ECO:0000313|Proteomes:UP000059672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LP1 {ECO:0000313|Proteomes:UP000059672};
RA   Wissuwa J., Le Moine Bauer S., Stokke R., Dahle H., Steen I.H.;
RT   "Complete genome sequence of Lutibacter profundus strain LP1.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMC09785.1, ECO:0000313|Proteomes:UP000059672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LP1 {ECO:0000313|EMBL:AMC09785.1,
RC   ECO:0000313|Proteomes:UP000059672};
RX   PubMed=27118569; DOI=10.1099/ijsem.0.001105;
RA   Le Moine Bauer S., Roalkvam I., Steen I.H., Dahle H.;
RT   "Lutibacter profundi sp. nov., isolated from a deep-sea hydrothermal system
RT   on the Arctic Mid-Ocean Ridge and emended description of the genus
RT   Lutibacter.";
RL   Int. J. Syst. Evol. Microbiol. 66:2671-2677(2016).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP013355; AMC09785.1; -; Genomic_DNA.
DR   RefSeq; WP_068205503.1; NZ_CP013355.1.
DR   AlphaFoldDB; A0A0X8G4A9; -.
DR   STRING; 1622118.Lupro_00235; -.
DR   KEGG; lut:Lupro_00235; -.
DR   PATRIC; fig|1622118.3.peg.50; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000059672; Chromosome.
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   Hydrolase {ECO:0000313|EMBL:AMC09785.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AMC09785.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059672};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          444..479
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          155..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  94864 MW;  FC9C64FE27C25D13 CRC64;
     MDDNFSPKVK DVITYSKEEA IRLGHDFIGT EHLMLGLLRK GDGKAIEILN SLEINLEHLR
     KKIEVLSPAN FSIDLSKEKK SIHLTRQAEK ALKTTFLEAK LYQNDAVNTA HLLLCILRNE
     NDPTTKLLHN FGVSYNDAKT VFKQLFSDQE LDLPKAENTS DDDFDTPKQN PFEQSKSNKP
     SDKKSKTPVL DNFGRDLTRL AEEGKLDPVV GRKKEIERVS QILSRRKKNN PMLIGEPGVG
     KSAIAEGLAL RIIERKVSRI LFNKRIVSLD LASLVAGTKY RGQFEERMKA LMNELEKNDD
     IILFIDEIHT IVGAGGATGS LDASNMLKPA LARGEIQCIG ATTLDEFRTN IEKDGALERR
     FQKIIVEPTS VDETIQILQN IKNKYEEHHN VDYTDEAIVA CVKLTNRYMT DRFLPDKAID
     AMDEAGSRIH ITNIVVPKEV LNLEAQLEKV KEDKSAAVNG QKYEEAARLR DDEKRIENLL
     LTEQIKWEEA SKLNREVVTQ DNVAEVVSMM TGIPVNRVAE AESKRLHDLP KLIKGKVIGQ
     NEAVSKVVKA IQRNRVGLKD PNKPIGSFIF LGQTGVGKTQ LAKVLATELF DSEDALVRID
     MSEYMEKFAI SRLIGAPPGY VGYEEGGQLT EKIRRKPYAV VLLDEIEKAH PDVFNMLLQI
     LDDGFITDSL GRRIDFRNTI IIMTSNIGSR QLKDFGAGVG FGTAAKASQA NAHAKSVIEN
     ALKKSFAPEF LNRIDDVVVF NALEREDIHS IIDIELSKLI ERIEDIGYNL QLTEEAKDYI
     ADKGFDKQYG ARPLKRAIQK YIEDTLAEEI VNSKLNEGDS IFMDLDKEKN ELTIKISKGK
     KKVE
//
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