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Database: UniProt
Entry: A0A5Q3LAG3_9BACT
LinkDB: A0A5Q3LAG3_9BACT
Original site: A0A5Q3LAG3_9BACT 
ID   A0A5Q3LAG3_9BACT        Unreviewed;       850 AA.
AC   A0A5Q3LAG3;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   03-MAY-2023, entry version 13.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:QGJ70707.1};
GN   ORFNames=PBC10988_24050 {ECO:0000313|EMBL:QGJ70707.1};
OS   Planctomycetales bacterium 10988.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales.
OX   NCBI_TaxID=2603660 {ECO:0000313|EMBL:QGJ70707.1, ECO:0000313|Proteomes:UP000352687};
RN   [1] {ECO:0000313|EMBL:QGJ70707.1, ECO:0000313|Proteomes:UP000352687}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10988 {ECO:0000313|EMBL:QGJ70707.1,
RC   ECO:0000313|Proteomes:UP000352687};
RX   PubMed=31644258;
RA   Panter F., Garcia R., Thewes A., Zaburannyi N., Bunk B., Overmann J.,
RA   Gutierrez M.V., Krug D., Muller R.;
RT   "Production of a Dibrominated Aromatic Secondary Metabolite by a
RT   Planctomycete Implies Complex Interaction with a Macroalgal Host.";
RL   ACS Chem. Biol. 0:0-0(2019).
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DR   EMBL; CP043547; QGJ70707.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5Q3LAG3; -.
DR   Proteomes; UP000352687; 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; 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; PS50151; UVR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:QGJ70707.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:QGJ70707.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:QGJ70707.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000352687};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          433..468
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          150..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          821..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          429..479
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        159..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   850 AA;  95420 MW;  C090C8FBAB23AB9A CRC64;
     MYERFTDRAR KVMQLANQEG QRFNHEYIGT EHVLLGLIKE GSGVAANVLK NLDVDLRKIR
     QEVEKLVQRG PGTPTPGKLP QTPRVKKVIE YSIEEAQNLN HNYVGTEHLL LGLLREKEGV
     AAQVLINLGL KLEEVRQEVL NLLGHVSDAD EGSEQLSATE EGEMASESPK SGKSKTPALD
     SFGRDLTELA RQGKLDPVIG REKEIERVTQ VLSRRTKNNP VLLGEAGVGK TAIVEGFAQR
     VIDGDVPESL SDRRIVVLDL AMMVAGTKYR GQFEERIKAV MNEVRRVQNT ILFIDEMHTL
     VGAGGAEGAI DAANVLKPSL ARGEIQCIGA TTLDEYRKHI EKDTALARRF QEVIVNPPSQ
     EEAVEILRGL RDRYEEHHRV RITDDALESS VELAARYITG RCLPDKAIDV IDEAGARVRL
     KAMTRPPDLK EIDEKIERLN KEKEEAVANQ DFEKAASFRD QAEKLKNRKK EIVQDWREQA
     NQTGGIVDEE VVSEVVSKMT GIPLTRMTTE ETQRLMAMED ELHRRVIGQD EAVKSISKAV
     RRSRSGLKDP KRPTGCFIFA GPTGVGKTLL AKALAEFMFG DEDALIQVDM SEYMEKHNVS
     RLVGAPPGYV GYEEGGQLTE KIRRRPYAVV LLDEIEKAHG DVFNMLLQVM EEGRLTDSFG
     RQVDFRNTIL IMTTNAGAEV ITRGESFGFQ RFDEDSTYQG MKDRVKDQIG KYFRPEFLNR
     VDDTIVFRQL QNADLQEIVD IELSKVRERL KDRGLELVLT DEAKELLVSR GSNVEYGARP
     LRRAIEHSVE DPLSEELLKG EFDENDTITV KVREVGEEKQ LYFEGSSSPK EPKEEVAHAS
     TSSEGTPSEE
//
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