ID A0A0P7BFB6_9BACT Unreviewed; 842 AA.
AC A0A0P7BFB6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:KPM49545.1};
GN ORFNames=AFM12_02780 {ECO:0000313|EMBL:KPM49545.1};
OS Jiulongibacter sediminis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Jiulongibacter.
OX NCBI_TaxID=1605367 {ECO:0000313|EMBL:KPM49545.1, ECO:0000313|Proteomes:UP000050454};
RN [1] {ECO:0000313|EMBL:KPM49545.1, ECO:0000313|Proteomes:UP000050454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN14-9 {ECO:0000313|EMBL:KPM49545.1,
RC ECO:0000313|Proteomes:UP000050454};
RA Liu Y., Du J., Shao Z.;
RT "The draft genome sequence of Leadbetterella sp. JN14-9.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPM49545.1}.
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DR EMBL; LGTQ01000005; KPM49545.1; -; Genomic_DNA.
DR RefSeq; WP_055143747.1; NZ_LGTQ01000005.1.
DR AlphaFoldDB; A0A0P7BFB6; -.
DR STRING; 1605367.AFM12_02780; -.
DR PATRIC; fig|1605367.3.peg.1899; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000050454; 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 Hydrolase {ECO:0000313|EMBL:KPM49545.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KPM49545.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050454};
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 442..477
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 146..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 842 AA; 94505 MW; 51587C28C24E6992 CRC64;
MEPKFSQRVK EVISLAREEA LRLGHDYIGT EHLILGMIRE GDGMGLELIR KTGIRIPDLK
QSIESATRGT ATNNIKNLAN IPLTRQSEKV LKITHLEAKI FKAEVIGTEH LLLAILRDGD
NLGCQILNRF KVNYELIKEM LEYQMTGESP RMDSPDTDDD DERSFASTGG SGQSREPKGA
EKSKTPILDN FGRDLTKLAD AGKLDQIIGR EKEIERVAQI LSRRKKNNPI LIGEPGVGKT
AIAEGLALRI VEKKVSRVLY GKRVVTLDLA SLVAGTKYRG QFEERMKAVM GELEKSPNVI
LFIDEIHTIV GAGGASGSLD ASNMFKPALA RGEIQCIGAT TLDEYRQYIE KDGALARRFQ
MVMVEPTTVE ETIEILHNIK DKYEDHHNVT YSDESIVSAV QYSERYISDR FLPDKAIDII
DEVGARVHIS NIHVPQEIID LEEAIEDIKV EKNAVVKSQR YEEAAQLRDK EKKLIDQLDR
VKEAWEEESK SKRHLVTEEN IGEVIAQITG IPINKVNMDE GERILKMGDA LKGRIIGQDG
AVKKLVKAIQ RTRVGLKDPK KPIGSFIFLG PTGVGKTELA KALTEYLFDR EDSLIRIDMS
EYMEKFSISR LVGAPPGYVG YEEGGQLTEK VRRKPYSVIL LDEIEKAHPD VFNILLQVLD
DGILTDSLGR KVDFRNTIII MTSNIGVRDL KDFGAGIGFA TKARKDNQEE AVKSTIQNAL
RKTFSPEFLN RLDDVIIFDS LGRESIHQII DLMLKKLFVR INSLGYEIEV TDKAKDFIAE
KGYDQQYGAR PLNRAIQKYV EDPLAEEILK GDVKEADILI VDYSGEGEEL TFSKKKEKAV
EQ
//
