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Database: UniProt
Entry: A0A0J5S487_9PAST
LinkDB: A0A0J5S487_9PAST
Original site: A0A0J5S487_9PAST 
ID   A0A0J5S487_9PAST        Unreviewed;       874 AA.
AC   A0A0J5S487;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Clp protease ClpV {ECO:0000313|EMBL:KMK51602.1};
GN   ORFNames=RO21_05305 {ECO:0000313|EMBL:KMK51602.1};
OS   Muribacter muris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Muribacter.
OX   NCBI_TaxID=67855 {ECO:0000313|EMBL:KMK51602.1, ECO:0000313|Proteomes:UP000036270};
RN   [1] {ECO:0000313|EMBL:KMK51602.1, ECO:0000313|Proteomes:UP000036270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ackerman80-443D {ECO:0000313|EMBL:KMK51602.1,
RC   ECO:0000313|Proteomes:UP000036270};
RA   Christensen H., Nicklas W., Bisgaard M.;
RT   "Reclassification of Actinobacillus muris as Muribacter muris.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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:KMK51602.1}.
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DR   EMBL; JWIZ01000027; KMK51602.1; -; Genomic_DNA.
DR   RefSeq; WP_047976755.1; NZ_JWIZ01000027.1.
DR   AlphaFoldDB; A0A0J5S487; -.
DR   STRING; 67855.RO21_05305; -.
DR   PATRIC; fig|67855.3.peg.926; -.
DR   Proteomes; UP000036270; 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; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017729; ATPase_T6SS_ClpV1.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03345; VI_ClpV1; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF182; CLP ATPASE; 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; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:KMK51602.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:KMK51602.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036270}.
FT   DOMAIN          216..362
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          605..771
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          771..863
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
SQ   SEQUENCE   874 AA;  96847 MW;  5FCD8D80F5DF33B9 CRC64;
     MLKIDLPVLV GKLHPIVKSV LEDVAADSIN AQITEITLPH LFKQLFATPL CDVRLIAEHF
     ELEIGTLIDA FELEVTQMKG KGGVEDYPRF SPLLVELLQD AWLLASAEMK QTELRSGVLF
     LALLLSSHRY LPHHLSQQFI TINRELLKRD WLLITASSAE APNVAKNPAN PTACSLTLLA
     KYAQDVTALA KQGQLDPVLC RDNEMDLMID ILCRRRKNNP IIVGEAGVGK SALIEGLALR
     IVNGEVPDKL CDTRIMSLDL GALQAGAAVK GEFEKRFKGV MAEIDQSPIP IILFIDEAHT
     LIGAGNQQGG LDVSNLLKPA LARGTLKTIA ATTWKEYKKY VEKDAALSRR FQLVKLNEPT
     VDEAIIIMQG LRLTYEQAHS VLIDEEAVIS AARLSDRYLS GRQLPDKAID VLDTACARVA
     ITLTSPPKAL SHLRTQIHQL ATEKTLFERA YRLGMSNDAE RLAALTNQID TLSYEQTLLE
     EKWHQQQELV KQIIAARQQL LEKEGNDDSD TGSLRATLQS LEIALSDAQK DQILVSPHVT
     KSQIETVIAE WTGVPLERLS QNELNIIADL PTYLSKEIKG QTLAIKHLHR HLLTARADLR
     RQGRPLGAFL LVGPSGVGKT ESVLQITNLL FGGKQYLTTI NMSEFQEKHT VSRLIGSPPG
     YVGYGEGGIL TEAIRRMPYS VVLLDEVEKA HPDVLNLFYQ AFDKGEMADG EGRLIDCQNV
     VFFLTSNLGY QTIVDNAENE SQLTTLLYPE LAAFFKPALL ARMEVIPFLP LSQTILADII
     DGKLSTLTAR LIERFNTSVT IDDDVKTEIL LRANRAENGA RMLESIIDGH MLPPISLLLL
     QKQAQNMPIE AIRFSVVDHQ FVAAIGEERC DFAI
//
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