ID A0A1H2YCW9_9BACL Unreviewed; 718 AA.
AC A0A1H2YCW9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpE {ECO:0000313|EMBL:SDX02815.1};
GN ORFNames=SAMN05444487_10925 {ECO:0000313|EMBL:SDX02815.1};
OS Marininema mesophilum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Marininema.
OX NCBI_TaxID=1048340 {ECO:0000313|EMBL:SDX02815.1, ECO:0000313|Proteomes:UP000198534};
RN [1] {ECO:0000313|EMBL:SDX02815.1, ECO:0000313|Proteomes:UP000198534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45610 {ECO:0000313|EMBL:SDX02815.1,
RC ECO:0000313|Proteomes:UP000198534};
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; FNNQ01000009; SDX02815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2YCW9; -.
DR STRING; 1048340.SAMN05444487_10925; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198534; 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; 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; 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:SF175; ATP-DEPENDENT CLP PROTEASE, ATP-BINDING SUBUNIT CLPC; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:SDX02815.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDX02815.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198534}.
FT DOMAIN 338..373
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 58..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 334..383
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 58..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 80046 MW; 9112559C2CE703AC CRC64;
MQCQHCKQHQ ATVDLHLQVN GQKKHLFLCQ ECYNQVKNQL TFPAGFPGGH PFQDFIQSFT
GHQPNSESTS NYNKQKQSTG GHGGGLLDQL GKNLNQAASS GLIDPVVGRD QEVDRVIETL
NRRNKNNPVL IGEPGVGKTA IAEGLALRIT QGQVPQKLKD KQIYLLDVAS LVANTGIRGQ
FEERMKQLIT ELQERQQIIL FIDEIHQLVG AGSAEGSQDA GNILKPALAR GELQVIGATT
LKEYRQIEKD AALERRFQPV MVNEPSIEEA IRILQGLRKN YEDYHSVAYT EDAIRASVQL
SHRYIQDRFL PDKAIDLMDE AGSKINLTSV TDSGAELREQ LTQITAEKEV ATQREEYERA
GQLRDEERKL EEQLEAIADQ TQRPVVDAET IQHLVELKTG IPVRRLQKDE QNKMKGLAEQ
LNAQVIGQTD AVEKVAKAIR RNRTGLRKGS RPIGSFLFVG PTGVGKTELA KTLAQELFGD
TDAMIRLDMS EFMEKHTVSK LIGSPPGYVG HEEAGQLTER VRRNPYSILL LDEIEKAHPD
VQHLFLQIME DGRLTDSQGR TVSFRDTLII MTSNAGVGMK PKMSIGFGNS PTEEKPTEIL
ESLADYFRPE FLNRLDGIIS FRSLSQKDLL RIVDLMLHDV IEVAEEQGIN LTVTDSAKLK
LAELGYHPAF GARPLRRVIE EHVEDGIADH MLDNDDVTSI LIDASDEKLT IMANVTSA
//