GenomeNet

Database: UniProt
Entry: A0A1S2PX35_9ACTN
LinkDB: A0A1S2PX35_9ACTN
Original site: A0A1S2PX35_9ACTN 
ID   A0A1S2PX35_9ACTN        Unreviewed;       838 AA.
AC   A0A1S2PX35;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Clp protease {ECO:0000313|EMBL:OIJ98389.1};
GN   ORFNames=BIV24_05960 {ECO:0000313|EMBL:OIJ98389.1};
OS   Streptomyces colonosanans.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1428652 {ECO:0000313|EMBL:OIJ98389.1, ECO:0000313|Proteomes:UP000179935};
RN   [1] {ECO:0000313|EMBL:OIJ98389.1, ECO:0000313|Proteomes:UP000179935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC 93 {ECO:0000313|EMBL:OIJ98389.1,
RC   ECO:0000313|Proteomes:UP000179935};
RA   Lee L.-H., Ser H.-L., Law J.W.-F.;
RT   "Genome sequence of Streptomyces sp. MUSC 93.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OIJ98389.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MLYP01000013; OIJ98389.1; -; Genomic_DNA.
DR   RefSeq; WP_071365091.1; NZ_MLYP01000013.1.
DR   AlphaFoldDB; A0A1S2PX35; -.
DR   STRING; 1428652.BIV24_05960; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000179935; 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; -; 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; 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   InterPro; IPR001943; UVR_dom.
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.
DR   PROSITE; PS50151; UVR; 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:OIJ98389.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:OIJ98389.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179935};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          36..176
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          439..474
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          152..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          814..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   838 AA;  90665 MW;  593AB699CDF1D8A4 CRC64;
     MTISPFGSGD PFSELFNRFF GMSPATSPPA VQRVPIGRLL SGSSQELLAA AGGRAAEDGS
     DLDTVHLLWA ATQVPAARQL LEQAGADPDR LAADLQESLP TGTGTGEPAL TPAAKRALLA
     AHARSQAAGA SYIGPEHILA ALLDDPRSPL TQTLRAEGAS PGALSGPARE GRPAGGHPDT
     PTLEQYGRDL TDEARSGRLD PVVGRAGEIE QTIEVLSRRT KNNPVLIGDP GVGKTAIVEG
     LAQRIVAEEV PKALKNRRVA ALEMAGLVAG SQYRGQFEER LKKVIDEVTQ AQKGIILFID
     ELHTVVGAGG TGEGSMDAGN ILKPALARGD LSVVGATTID EYRKHIEKDA ALERRFQPVM
     VPEPTVEETI EILRGLRDSY EAHHQVRYTD EALDAAASLS DRYISDRFLP DKAIDLMDQA
     GARVGLRSVG GSREAAELED RLSRLRREKD EAVSTEDFTR AGELKREVTE LEERLGSMGE
     GGVPTPAVTP EDIAEVLSAR TGIPVSQLTE TERERLLKLE EVLHERVIGQ DQAVTAVAQA
     VRRGRAGMGD PDRPTGSFLF LGPTGVGKTE LAKALAELLF GDPDRMVRFD MSEFQEKHTV
     SRLIGSPPGY VGYEEAGQLT EAVRRKPYSV VLFDEVEKAH RDVFNLLLQV LDDGRLTDAK
     GRTVDFRNTV VIMTSNIASK RILDHHGDVE EIKDDLMAEL QAHFRPEFLN RIDEVIVFHA
     LVREDLVRIV DLLLEGSRRR LHAQQVGLEV TEAAKDWLAE RGYQPEYGAR PLRRTIQSEL
     DNRLSNMLLD GTLNPGDTVV ADVADDELVL GLKAKPATDD KAAPGEGGAQ GSPEGCER
//
DBGET integrated database retrieval system