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Database: UniProt
Entry: A0A5A7SBS2_9NOCA
LinkDB: A0A5A7SBS2_9NOCA
Original site: A0A5A7SBS2_9NOCA 
ID   A0A5A7SBS2_9NOCA        Unreviewed;       852 AA.
AC   A0A5A7SBS2;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:KAA0022043.1};
GN   ORFNames=FOY51_16850 {ECO:0000313|EMBL:KAA0022043.1};
OS   Spelaeibacter cavernicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Spelaeibacter.
OX   NCBI_TaxID=2495913 {ECO:0000313|EMBL:KAA0022043.1, ECO:0000313|Proteomes:UP000322244};
RN   [1] {ECO:0000313|EMBL:KAA0022043.1, ECO:0000313|Proteomes:UP000322244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C1-24 {ECO:0000313|EMBL:KAA0022043.1,
RC   ECO:0000313|Proteomes:UP000322244};
RA   Lee S.D.;
RT   "Rhodococcus cavernicolus sp. nov., isolated from a cave.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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:KAA0022043.1}.
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DR   EMBL; VLNY01000007; KAA0022043.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5A7SBS2; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000322244; 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: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; 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:SF193; CHAPERONE PROTEIN CLPB; 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; PS50151; UVR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:KAA0022043.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:KAA0022043.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:KAA0022043.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000322244};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          2..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          424..459
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          145..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          813..852
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..828
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   852 AA;  94304 MW;  4177DDC00FAB3B41 CRC64;
     MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKSLE SLGISLEGVR
     SQVEEIIGQG QQAPSGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGVA
     AQVLVKLGAD LNRVRQQVIQ LLSGYQGKEP SESGSGRGGE AGTPSTSLVL DQFGRNLTQA
     ALEGKLDPVI GRAKEIERVM QVLSRRTKNN PVLIGEPGVG KTAVVEGLAQ AIVNGEVPET
     LKDKQLYTLD LGSLVAGSRY RGDFEERLKK VLKEINTRGD IILFIDELHT LVGAGAAEGA
     IDAASILKPK LARGELQTIG ATTLDEYRKY IEKDAALERR FQPVQVGEPT VEHTIDILKG
     LRDRYEAHHR VSITDSALVA AATLADRYIN DRFLPDKAID LIDEAGARMR IRRMTAPPDL
     REFDDKIADA RREKESAIDA QDFEKAANLR DKEKTLVAQR AEREKQWRSG DLDVIAEVDD
     EQIAEVLANW TGIPVFKLTE EETTRLLRME DELHKRIIGQ EEAVKAVAKA IRRTRAGLKD
     PKRPSGSFIF AGPSGVGKTE LSKALANFLF GDDDALIQID MGEFHDRFTA SRLFGAPPGY
     VGYEEGGQLT EKVRRKPFSV VLFDEIEKAH QEIYNTLLQV LEDGRLTDGQ GRTVDFKNTV
     LIFTSNLGTS DISKAVGLGF AQSNVEGSNY ERMKMKVNDE LKKHFRPEFL NRIDDIVVFH
     QLTTDQIVQM VDLMIARVGR QLAAKDMVME LTDKAKSLLA KRGFDPVLGA RPLRRTIQRE
     IEDQLSEKIL FNELTPGQIV FVDVDNWDGE GQGEDAKFTF RGEQKPVHVP DSPEGVLAGA
     SESGSSSESI GE
//
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