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Database: UniProt
Entry: G6EBK3_9SPHN
LinkDB: G6EBK3_9SPHN
Original site: G6EBK3_9SPHN 
ID   G6EBK3_9SPHN            Unreviewed;       790 AA.
AC   G6EBK3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:EHJ61285.1};
GN   Name=clpA {ECO:0000313|EMBL:EHJ61285.1};
GN   ORFNames=NSU_1724 {ECO:0000313|EMBL:EHJ61285.1};
OS   Novosphingobium pentaromativorans US6-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1088721 {ECO:0000313|EMBL:EHJ61285.1, ECO:0000313|Proteomes:UP000004030};
RN   [1] {ECO:0000313|EMBL:EHJ61285.1, ECO:0000313|Proteomes:UP000004030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=US6-1 {ECO:0000313|EMBL:EHJ61285.1,
RC   ECO:0000313|Proteomes:UP000004030};
RX   PubMed=22275104; DOI=10.1128/JB.06476-11;
RA   Luo Y.R., Kang S.G., Kim S.J., Kim M.R., Li N., Lee J.H., Kwon K.K.;
RT   "Genome sequence of benzo(a)pyrene-degrading bacterium Novosphingobium
RT   pentaromativorans US6-1.";
RL   J. Bacteriol. 194:907-907(2012).
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:EHJ61285.1}.
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DR   EMBL; AGFM01000024; EHJ61285.1; -; Genomic_DNA.
DR   RefSeq; WP_007012639.1; NZ_CP009291.1.
DR   AlphaFoldDB; G6EBK3; -.
DR   STRING; 1088721.JI59_11460; -.
DR   KEGG; npn:JI59_11460; -.
DR   PATRIC; fig|1088721.3.peg.1703; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000004030; 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:EHJ61285.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EHJ61285.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004030};
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          144..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          754..790
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   790 AA;  87139 MW;  B35655D5655C98AD CRC64;
     MPSFAQSLEK TLHSALSHAS ERSHEYATLE HLLLALIDDP DAAQVMQACG VDLGDLGDVV
     RQYLDQEYQS LKTEEKGDPA PTAGFQRVIQ RAILHVQSSG KDTVTGANVL VALFSERDSY
     AVYFLQQQDM SRLDAVSYIS HGIGKGGKRI EDRSPKGSEE QTPTPEEKAE TKAANKKDSA
     LDQFCVNLNE KALAGKVDPL IGRGPEVDRT IQILCRRSKN NPLYVGDPGV GKTAIAEGLA
     RKIVEGEVPE VLSEAVIYSL DMGSLLAGTR YRGDFEERLK QVVAELEKMP HAILFIDEIH
     TVIGAGATSG GAMDASNLLK PALSGGTIRC IGSTTYKEFR NHFEKDRALL RRFQKIDVNE
     PTVEDTVKIL KGLRTAFEDH HGVRYTPDAI KTAVELSARY INDRKLPDKA IDVIDEVGAM
     QMLVPPSRRK KTITAREIEQ VIATMARIPP KSVSSDDKKA LENLERDLKR VVFGQDKAIE
     VLSTAMKLSR AGLRDPDKPI GSFLFSGPTG VGKTEVAKQL ATIMGIPMQR FDMSEYMERH
     SVSRLIGAPP GYVGFDQGGL LTDAIDQQPH CVLLLDEIEK AHPDLFNILL QVMDNGKLTD
     HHGKTVDFRN VVLIMTTNAG ASDMAKQGIG FGDTSKADAG EEAVKQMFSP EFRNRLDAIV
     PFAYLAKETI SRVVDKFILQ LELQLADQNV HIQFDSDARE WLGHRGYDRL YGARPMARVI
     QERVKQPLAE ELLFGKLAHG GEVHVSVKED ALNFELTPAP PKETKSRKKK APAKKPVRKT
     GPQPEENTDD
//
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