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
//