ID A0A173MCT6_9BACT Unreviewed; 825 AA.
AC A0A173MCT6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:SIT21710.1};
GN ORFNames=SAMN05421788_105180 {ECO:0000313|EMBL:SIT21710.1};
OS Filimonas lacunae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Filimonas.
OX NCBI_TaxID=477680 {ECO:0000313|EMBL:SIT21710.1, ECO:0000313|Proteomes:UP000186917};
RN [1] {ECO:0000313|Proteomes:UP000186917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21054 {ECO:0000313|Proteomes:UP000186917};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FTOR01000005; SIT21710.1; -; Genomic_DNA.
DR RefSeq; WP_076380021.1; NZ_FTOR01000005.1.
DR AlphaFoldDB; A0A173MCT6; -.
DR STRING; 477680.SAMN05421788_105180; -.
DR KEGG; fln:FLA_1372; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000186917; 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; IPR001270; ClpA/B.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:SIT21710.1};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:SIT21710.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:SIT21710.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186917}.
FT DOMAIN 205..347
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 564..730
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 732..822
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 410..437
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 825 AA; 92038 MW; DD62B837823F2962 CRC64;
MNILFANDTV KEVLHIAQAI ARENYHATYG APHLLRALMH KETGLHDFLH SLEKDPAYFI
EWAEVRMEDF PSTMSLPETI EQAPEIEDIL EEADDIRVKL GLDEVTALCV LTALVKPHVV
FTPAQLKSLP LREGEIIASL KGTSENNATP LNGVNGKSEQ HYGSDSALHK YCVNKTALAQ
SKTIDPIIGR EKETRMLIEV LGRRNKPNVI ITGEPGVGKT ALVDGLAYEI IAGNVPLHIQ
HAVLLELDMG TLMAGASYKG EVEDRLKKII TELKKLDKAI LFIDEIHQLL DSKGALGSGT
ANLLKPELAR GAITVIGATT SEEHRKIIEP DQAFSRRFEV LAIYEPDADT CYKMIEFLIP
RYEAHHHIKI APDAIAECVR LSKRYLKEKC LPDAALDLLD RTMSAIRMLD ETSAKELQQW
KDKYEALKAE SNEGEQASLR DYKWHYQLLQ NMVSPILWGS LQEQPDISAI ESVAELQQLT
EKTFAELDTL KEIKRDTVGK QELAAVMAAK TNIPIGKIQA KEKEKLLNME TALQRRVVGQ
DHALKVLSDA IVQSRSGIHK PGQPIGSFFL LGPTGTGKTE LAKSIAELLF NDEKAMIRFD
MSEFKEEHSA ALLYGAPPGY VGYEEGGMLV NKIRRQPYSV VLFDEIEKAH PSVFDVFLQI
MDEGKVTDKL GKEGDFSNAL ILFTSNIGSQ FIVEKFEQQV IPTSRELMDI MARNFRPEFL
ARITEILPFA PVNEAMAVNI FNIQLTSLLN PLHRLGIALN ITDDARKQLA LSGFSPQYGA
RQISGVIRSQ LSRPISRMIV NEEVQKGHTI VVSLDAEGQL QWNVQ
//