ID A0A1H6K1D4_9FLAO Unreviewed; 847 AA.
AC A0A1H6K1D4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SEH68626.1};
GN ORFNames=SAMN02927937_00875 {ECO:0000313|EMBL:SEH68626.1};
OS Paenimyroides aquimaris.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Paenimyroides.
OX NCBI_TaxID=1159016 {ECO:0000313|EMBL:SEH68626.1, ECO:0000313|Proteomes:UP000199634};
RN [1] {ECO:0000313|EMBL:SEH68626.1, ECO:0000313|Proteomes:UP000199634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10825 {ECO:0000313|EMBL:SEH68626.1,
RC ECO:0000313|Proteomes:UP000199634};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNXE01000008; SEH68626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6K1D4; -.
DR STRING; 1159016.SAMN02927937_00875; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199634; 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: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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:SEH68626.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEH68626.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199634};
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 446..481
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 154..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 442..488
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 847 AA; 95349 MW; 81E16B59C8116590 CRC64;
MDDNFSPRVK EVITFSRDEA LRLGHDYIGT EHIMLGILRE SQGEAITILQ NLSIDLDFLK
NRFEALIPEN PNKIINTEKK NIHLTKQAEN ALKRAFLEKK LYKTDMINTG HILMSILRNT
EDPTTILLNR CKVDYDNAKQ EFVSLLSNSE SLSEQPLNSA FDDDERGDSM SDNFNNPSAG
NKAGKKSKTP VLDNFGRDLT ELAEEGKLDP VVGREKEIER VSQILSRRKK NNPLLIGEPG
VGKSAIAEGL ALRIIQKKVS RILFNKRVVT LDLASLVAGT KYRGQFEERM KAVMNELEKN
DDIILFIDEI HTIVGAGGAT GSLDASNMFK PALARGEIQC VGATTLDEYR QYIEKDGALE
RRFQKVIVEP TSEEETIIIL NNIKPKYEDH HNVIYTPEAI EACVKLTSRY MTDRFLPDKA
IDALDEAGSR VHITNIEVPD DILKLEKELE EVRDKKTDAV KRQKYEEAAA LRDDEKRIEK
DLAVAQERWE EDSKNNKITV TEEHVADVVS MMTGIPVNKI AQAESKKLAT LPDAIKGKVI
GQDEAVAKIA KSIQRNRAGL KDPNKPIGSF IFLGQTGVGK TQLAKVIAKE IFDSEDALIR
IDMSEYMEKF AISRLVGAPP GYVGYEEGGQ LTEKVRRKPY SVILLDEVEK AHPDVFNMLL
QVLDDGHLTD SLGRKIDFRN TIIIMTSNIG ARQLKDFGTG VGFGTKSKQE QQEELSKSVI
ENALKKAFAP EFLNRIDDVI VFNALEKEDI HKIINIEIEK LYQRVNNLGY QLELTAEALD
FIADKGFDKQ YGARPLKRAI QKYVEDLLAE EIINGNIHEN DVLLMDKIKD EDELKVTVKN
TNSSLKN
//
