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Database: UniProt
Entry: A0A1I7NHL5_9BACT
LinkDB: A0A1I7NHL5_9BACT
Original site: A0A1I7NHL5_9BACT 
ID   A0A1I7NHL5_9BACT        Unreviewed;       851 AA.
AC   A0A1I7NHL5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SFV34148.1};
GN   ORFNames=SAMN05660895_1917 {ECO:0000313|EMBL:SFV34148.1};
OS   Thermoflavifilum thermophilum.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Thermoflavifilum.
OX   NCBI_TaxID=1393122 {ECO:0000313|EMBL:SFV34148.1, ECO:0000313|Proteomes:UP000199537};
RN   [1] {ECO:0000313|Proteomes:UP000199537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14807 {ECO:0000313|Proteomes:UP000199537};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; FPCJ01000001; SFV34148.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7NHL5; -.
DR   STRING; 1393122.SAMN05660895_1917; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000199537; 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:SFV34148.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFV34148.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199537};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          441..476
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          148..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          437..487
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        172..186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   851 AA;  96322 MW;  1759B40BB8413753 CRC64;
     MDQNFSPQVK EIISFSREEA LRLGNDFIGT EHLLLGLIRE GESTAIQILK SMNVNIEELK
     REVEAAVRDK TGKNIANINS LPLTKQAEKV IRVTVLEAKS MKSPTVETEH LMLSILKNKE
     NICTQLLKQY DVDYESFKSE LGYVKSSDPK AEYSDETGEE EFDEERKSSY SSRTTRQAST
     KSKTPVLDNF GRDITRLAEL GQLDPIVGRE KEIERVSQIL SRRKKNNPIL IGEPGVGKTA
     IVEGLALRIV QRKVSRVLFD KRVVSLDLAA LVAGTKYRGQ FEERMKAIMN ELEKNRDVIL
     FIDEIHTIIG AGGASGSLDA SNIFKPALAR GELQCIGAST LDEYRMYIEK DGALDRRFQK
     VMIDPPTPEE TIQILMNIKS RYEEFHNVDY SEEAIQACVR LSDRYITDRF LPDKAIDVMD
     EVGARVHLKN INVPQHILDL EKKIEEIKQE KNRVVKSQRF EEAAALRDTE KKLGEELERA
     KAEWEEEIKH RRYPITEEDV AEVVSMMTGI PVKRMVQAES EKLLHMADDL RQAVVGQDEA
     ILKVTKAIQR NRVGLKDPRK PIGSFIFLGP TGVGKTELAK ALARYLFDSE DALIRIDMSE
     YMEKFSVSRL IGAPPGYVGY EEGGQLTEKV RRKPYSVVLL DEIEKAHPDI YNILLQVLDD
     GHLTDGLGRK VDFKNTLIIM TSNIGVRQLK DFGAGVGFVT AARSNEEENT RAVIEKALKR
     TFSPEFLNRI DDVVIFNPLS KEHIFAIIDI IMKDVHKRLE NMGVKLELTQ AAKEFLADKG
     YDTQFGARPL HRAIQKYLED PLAEEILMLK VKQGDVLIAD FDEKNQALKF RLKLSEPEVS
     SASSPATEKK S
//
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