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Database: UniProt
Entry: A0A1E7JXJ6_9ACTN
LinkDB: A0A1E7JXJ6_9ACTN
Original site: A0A1E7JXJ6_9ACTN 
ID   A0A1E7JXJ6_9ACTN        Unreviewed;       930 AA.
AC   A0A1E7JXJ6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Clp protease ClpB {ECO:0000313|EMBL:OEU96389.1};
GN   ORFNames=AN216_20525 {ECO:0000313|EMBL:OEU96389.1};
OS   Streptomyces oceani.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1075402 {ECO:0000313|EMBL:OEU96389.1, ECO:0000313|Proteomes:UP000176101};
RN   [1] {ECO:0000313|EMBL:OEU96389.1, ECO:0000313|Proteomes:UP000176101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 02100 {ECO:0000313|EMBL:OEU96389.1,
RC   ECO:0000313|Proteomes:UP000176101};
RX   PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA   Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA   Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT   "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT   Adaptation to the Marine Environment and Their Diversity at the Genomic
RT   Level.";
RL   Front. Microbiol. 7:998-998(2016).
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
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:OEU96389.1}.
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DR   EMBL; LJGU01000141; OEU96389.1; -; Genomic_DNA.
DR   RefSeq; WP_070198173.1; NZ_LJGU01000141.1.
DR   AlphaFoldDB; A0A1E7JXJ6; -.
DR   STRING; 1075402.AN216_20525; -.
DR   PATRIC; fig|1075402.3.peg.289; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000176101; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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:SF18; HEAT SHOCK PROTEIN 104; 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; 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   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Hydrolase {ECO:0000313|EMBL:OEU96389.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:OEU96389.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176101};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   930 AA;  100444 MW;  130697774CAD4657 CRC64;
     MDAELTNKSR DAISTANDRA VRDGHPDITP AHLLLALLEG EDNENIQDLL AAAEADQAAL
     RAGAERQLAA LPSVQGSTVA RPQPNRALLA VIADATDRAK ELGDDYVSTE HLLIGLATKG
     EATGTLLKEQ GAADRKLLDA FAAARGSQRV TNADPEGTYK ALEKFGTDFT AAARDGKLDP
     VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVKGDVP ESLKDKRLVG
     LDIGAMVAGA KYRGEFEERL KTVLAEIKSS DGRVITFIDE LHTVVGAGAG GDSAMDAGNM
     LKPMLARGEL RMVGATTLDE YRERIEKDPA LERRFQQVLV AEPTVGDSIA ILRGLKGRYE
     AHHKVQIADG ALVAAAALSD RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PVEIDELQRA
     VDRLRMEELA LANETDPGSV ERLARLRREL ADREEELRGL TARWEKEKQS LNQLGELKER
     LDEARGQAER AQRDGDFEGA SQLLYGEIPD LERRLEAATA AEKASAATAA EQASAATAAE
     QASAATAAEQ ASAATAAEKA SAATAAEQDS GATAAEQEQA ASGGARGSAG EKPTMVKEEV
     GQDDIAEVVA SWTGIPAGRL LEGETRKLLR MEEELGRRLI GQAPAVRSVS DAVRRTRAGI
     ADPDRPTGSF LFLGPTGVGK TELAKALADF LFDDERAMVR IDMSEYGEKH SVARLVGAPP
     GYVGYEEGGQ LTEAVRRRPY SVVLLDEVEK AHHEVFDILL QVLDDGRLTD GQGRTVDFRN
     TILILTSNLG SQHLTNPLVK EEEQQEKVLD AVRAAFRPEF LNRLDDVVVF SALSQEELSR
     IAALQLDGLQ RRLSERRLEL DVTPAALDWL AREGMDPAYG ARPLRRLVQT AIGDQLAREI
     LSGEVRDGDT VRVDRVEGWD GLSVGPAERG
//
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