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Database: UniProt
Entry: A0A4V2NMD8_9GAMM
LinkDB: A0A4V2NMD8_9GAMM
Original site: A0A4V2NMD8_9GAMM 
ID   A0A4V2NMD8_9GAMM        Unreviewed;       756 AA.
AC   A0A4V2NMD8;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:TCI12847.1};
GN   Name=clpA {ECO:0000313|EMBL:TCI12847.1};
GN   ORFNames=EZM97_05855 {ECO:0000313|EMBL:TCI12847.1};
OS   Dyella soli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=522319 {ECO:0000313|EMBL:TCI12847.1, ECO:0000313|Proteomes:UP000291822};
RN   [1] {ECO:0000313|EMBL:TCI12847.1, ECO:0000313|Proteomes:UP000291822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC 12747 {ECO:0000313|EMBL:TCI12847.1,
RC   ECO:0000313|Proteomes:UP000291822};
RA   Gao Z.-H., Qiu L.-H.;
RT   "Dyella amyloliquefaciens sp. nov., isolated from forest soil.";
RL   Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, 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:TCI12847.1}.
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DR   EMBL; SJTG01000001; TCI12847.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4V2NMD8; -.
DR   Proteomes; UP000291822; 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:0043335; P:protein unfolding; IEA:InterPro.
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   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; IPR013461; ClpA.
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   NCBIfam; TIGR02639; ClpA; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 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; PS51903; CLP_R; 1.
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   Hydrolase {ECO:0000313|EMBL:TCI12847.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TCI12847.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291822};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          147..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   756 AA;  83135 MW;  312F317F31827537 CRC64;
     MFSKDLEVTI GQCYKQAREQ RHEFMTVEHL LLALTDNQSA LGALRACGVD LPRLTHELEK
     IIAETVPVLP HGDERDTQPT LGFQRVLQRA VYHVQSSGRK EVTGANVLVA IFGEKDSHAV
     YFLHQQEITR LDVVNYISHG IAKIGDEPSA GMSGAEREGE EGGESRGNPL SEYASNLNEL
     ALEGKIDPLI GRQDEIERTI QVLCRRRKNN PLYVGEAGVG KTALAEGLAK RIVDGDVPEV
     LENATIWSLD LGALVAGTKY RGDFEKRLKA VISQLKKQQG AILFIDEIHT IIGAGSASGG
     TMDASNLIKP MLASGELRCI GSTTFQEFRG IFEKDRALAR RFQKIDVVEP TVADSIEILK
     GLRSRFEEHH NVVYTNESLK AAVDLSVKHI PDRLLPDKAI DIIDEAGARQ RLLPADQRTG
     KIDVPEVEYI VAKMARIPAK QVSASDRDVL RNLERNLKMV VFGQDAAIEA LAASIKMARS
     GLADPAKPIG SFLLAGPTGV GKTEVTRQLA MQLGIEMIRF DMSEYMEAHS VSRLVGAPPG
     YVGFDQGGLL TEAVTKHPHA VLLLDEIEKA HPDVYNILLQ VMDRGVLTDT NGREANFKNV
     VVVMTTNAGA QQASRRGIGF VKQSHQMDAM EVIRRTFTPE FRNRLDAIIQ FNALDFDHIL
     RVVDKFIIEL ESQLSEKHVT LDVDADARRW LAEHGFDPQM GARPMARVIQ EKVKRALADE
     LLFGKLAEGG KVHLSVADGE LKVDTEAAAP VPAEVS
//
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