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Database: UniProt
Entry: D1PMW0_9FIRM
LinkDB: D1PMW0_9FIRM
Original site: D1PMW0_9FIRM 
ID   D1PMW0_9FIRM            Unreviewed;       759 AA.
AC   D1PMW0;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=ATPase family associated with various cellular activities (AAA) {ECO:0000313|EMBL:EFB75895.1};
GN   ORFNames=SUBVAR_05674 {ECO:0000313|EMBL:EFB75895.1};
OS   Subdoligranulum variabile DSM 15176.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Subdoligranulum.
OX   NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB75895.1, ECO:0000313|Proteomes:UP000003438};
RN   [1] {ECO:0000313|EMBL:EFB75895.1, ECO:0000313|Proteomes:UP000003438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB75895.1,
RC   ECO:0000313|Proteomes:UP000003438};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (DEC-2009) 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:EFB75895.1}.
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DR   EMBL; ACBY02000023; EFB75895.1; -; Genomic_DNA.
DR   RefSeq; WP_007047055.1; NZ_GG704769.1.
DR   AlphaFoldDB; D1PMW0; -.
DR   STRING; 411471.SUBVAR_05674; -.
DR   GeneID; 78305862; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000003438; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   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   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; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003438};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          203..347
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          485..662
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          661..750
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
SQ   SEQUENCE   759 AA;  81674 MW;  04633F14CDFC054B CRC64;
     MLFHCYKGFS RAAAHTLHTA VILAGRQGCS AADTGHLLLA MLQTAQGPAA DFLRRKRVTE
     SALRSCVQAR SCSGTPRSLG KQDLAPETRK AMEFAVLGAH AASAARAENE HLLCAMLEDS
     SCTASVWLAS LGIEVPQAAR ECRQLSGQLV LPAQPRMATT RGGKASEKYG RDLTRLAQEG
     RLDPVLCRDA ELDRMIEILC RRQKNNPCLL GEPGVGKSAL AEALAQRIAS GQITPSLRNK
     RVLALDMASM VAGTKYRGDF EERFKNLLEE LYRDNSTILF IDEIHVIAGA GAAEGAIDAA
     SILKPMLARG EIQLIGATTV EEYRKTIQKD SALERRFGKV MVEEPSPADA ETILRGLMPR
     YERYHGIAIP QEAIHAAVEL SVRYLPGRYL PDKAIDLLDE AAASVRIAGA EGGGKQRALQ
     PSDVAKVVSE ASGVPAERVG EAERERLANL ESRLAAEVIG QPKAVAAVAA AIRRSRTGLR
     EAGRPIGAML FLGPTGVGKT QLARTLAKCW FGSEKALLRF DMSEYMERHT VARLIGAPPG
     YVGHDEGGQL TEAVRRRPYS VVLFDEIEKA HGDIQNLLLQ ILEDGSLTDS QGRKADFSNT
     IILLTSNLGA RCLSGQTAPM GFGAAGSETA RRGKQAIQEA KEFFRPELMG RLDETVLFEP
     LGPQQLAAIA DRLLCELEER AARQGYTLHH TAAAARCLAG DKVPPYGARE LRRTVSRAVE
     QALADRIAAG TARAGAVYTA DAAPDGSIVL QETDLAACV
//
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