ID A0A2W2ACG8_9BACT Unreviewed; 847 AA.
AC A0A2W2ACG8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:PZF72991.1};
GN ORFNames=DN068_11315 {ECO:0000313|EMBL:PZF72991.1};
OS Taibaiella soli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Taibaiella.
OX NCBI_TaxID=1649169 {ECO:0000313|EMBL:PZF72991.1, ECO:0000313|Proteomes:UP000248745};
RN [1] {ECO:0000313|EMBL:PZF72991.1, ECO:0000313|Proteomes:UP000248745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1-15 {ECO:0000313|EMBL:PZF72991.1,
RC ECO:0000313|Proteomes:UP000248745};
RA Kim M.-K., Park S., Kim T.-S., Joung Y., Han J.-H., Kim S.B.;
RT "Mucibacter soli gen. nov., sp. nov., a new member of the family
RT Chitinophagaceae producing mucin.";
RL Submitted (JUN-2018) 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:PZF72991.1}.
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DR EMBL; QKTW01000016; PZF72991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2ACG8; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000248745; 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:PZF72991.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PZF72991.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248745};
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 147..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 437..487
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 847 AA; 95475 MW; 07967E8563111A0F CRC64;
MDSNFSPKVK EIISYSREEA LRLGNDFIGT EHLLLGLIRE GDGLAVRVLQ SMQVDLYDLR
KELEMAIKDK NNKPMANINS LPLTKQAEKV IRITVLEAKA LKSPTVETEH LMLSILKNKE
NVATQILHQY DVDYDRFKNE LSILQGHAPT ADYGSDPGSE EFEEDDERRQ FQQRRPAGNA
KSKTPVLDNF GRDITKLAEM GNLDPIVGRE EEIERVSQIL SRRKKNNPIL IGEPGVGKTA
IVEGLALRIV QRKVSRVLFD KRVISLDLAA LVAGTKYRGQ FEERMKAIMN ELEKNRDVIL
FIDEIHTIVG AGGASGSLDA SNIFKPALAR GDLQCIGAST LDEYRMYIEK DGALDRRFQK
VMVDPPSVDE TITILNNIRS KYEEFHNVSY DQEAIEACVK LSDRYMTDRL LPDKAIDVMD
EVGARVHLKN INVPQNILEL EKKIEDIKQE KNKVVKSQRF EEAAALRDKE KRLGEELEKA
KADWEEEAKN KRYPIHEEDI AEVVSMMTGI PVMRMVEAES AKLRRMGEDL KGAVVGQDEA
ISKVVKAIQR NRVGLKDPRK PIGSFIFLGP TGVGKTELAR ALARYMFDSE DALIRVDMSE
YMEKFSLSRL IGAPPGYVGY EEGGQLTEKV RRKPYSVVLL DEIEKAHPDI FNIMLQVLDD
GQLTDGLGRK VDFKNTLIIM TSNIGVRQLK DFGDGVGFAT SAKAVAAEDS TRGVIEKALK
RTFSPEFLNR IDDVVIFNSL DQGHINQIID IIMKDVMKRL NTLGFGLELT DGAKKYIAEK
GYDQAFGARP LHRAIQKYLE DPLAEEILNH RIKEGDAVIA DYDEEEKKIV FTIDHTPAKK
ETTSTQE
//