ID A0A1I1F9K9_9BACT Unreviewed; 841 AA.
AC A0A1I1F9K9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SFB96065.1};
GN ORFNames=SAMN05421780_102106 {ECO:0000313|EMBL:SFB96065.1};
OS Flexibacter flexilis DSM 6793.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flexibacteraceae;
OC Flexibacter.
OX NCBI_TaxID=927664 {ECO:0000313|EMBL:SFB96065.1, ECO:0000313|Proteomes:UP000199514};
RN [1] {ECO:0000313|EMBL:SFB96065.1, ECO:0000313|Proteomes:UP000199514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6793 {ECO:0000313|EMBL:SFB96065.1,
RC ECO:0000313|Proteomes:UP000199514};
RA de Groot N.N.;
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; FOLE01000002; SFB96065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1F9K9; -.
DR STRING; 927664.SAMN05421780_102106; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199514; 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:SFB96065.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFB96065.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199514};
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 442..477
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 143..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 438..488
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 841 AA; 93380 MW; F96060C8D3EB7650 CRC64;
MEAKFSNRVK EVISLSREEA LRLGHEYIGS EHLLLGMIRE GEGIAISLLK KLGADLDEVR
MAIEHATKGT ATGNVKNLES IPLTRQSEKV LKLTYLEARS YKSEIIGTEH LLLSILRDAD
SVASQILARF DINYEGVREV LGPLPNRPTA GHDAGDDDDD SSRTFGGGSG NKDTSKAAGA
EKSRTPVLDN FGRDLTKAAE EGKLDPIVGR EKEIERVAQI LSRRKKNNPI LIGEPGVGKT
AIAEGLALRI IQKKVSRVLF GKRVITLDLA SLVAGTKYRG QFEERMKAVM NELEKSPEVI
LFIDEIHTIV GAGGASGSLD ASNMFKPALA RGDIQCIGAT TLDEYRQYIE KDGALARRFQ
MVMVDATTPE ETVQILDNIK EKYESHHHVN YTPEAIEACV KLSDRYISDR FLPDKAIDVL
DEAGARVHIN NIHVPDDIVE LEAQIEDVKK EKNRVVKSQK YEEAAALRDK EKRLNESLES
AKSRWEEETR SKRYTVNEEN VAEVIGMMTG IPTNRIAQTE GQKLLSMGKD LKGKVIGQDE
AIAKLVKAIQ RTRVGLKDPK KPIGSFVFLG PTGVGKTELA KVLATYLFDK EDALVRIDMS
EYMEKFSVSR LVGAPPGYVG YEEGGQLTEK IRRKPYSVVL LDEIEKAHPD VFNILLQVLD
DGILTDGLGR RVDFRNTIII MTSNIGIREL KDFGTGIGFS TKAKADNVDT EMKNTIQNAL
RKAFSPEFLN RLDDVIIFNS LQREHIHQII DISLSKLFGR ITSMGYNIEL TEKAKDFIAE
KGYDQQFGAR PLNRAIQKYL EDPIAEEILK GEVQMGDTLL ADHAEGEEGL TVTVKKPATE
V
//