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Database: UniProt
Entry: A0A3A9ZLM7_9ACTN
LinkDB: A0A3A9ZLM7_9ACTN
Original site: A0A3A9ZLM7_9ACTN 
ID   A0A3A9ZLM7_9ACTN        Unreviewed;       850 AA.
AC   A0A3A9ZLM7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit {ECO:0000313|EMBL:RKN48644.1};
GN   ORFNames=D7223_11765 {ECO:0000313|EMBL:RKN48644.1};
OS   Micromonospora endolithica.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=230091 {ECO:0000313|EMBL:RKN48644.1, ECO:0000313|Proteomes:UP000281726};
RN   [1] {ECO:0000313|EMBL:RKN48644.1, ECO:0000313|Proteomes:UP000281726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 12677 {ECO:0000313|EMBL:RKN48644.1,
RC   ECO:0000313|Proteomes:UP000281726};
RX   PubMed=15046305; DOI=10.1078/072320204322881781;
RA   Hirsch P., Mevs U., Kroppenstedt R.M., Schumann P., Stackebrandt E.;
RT   "Cryptoendolithic actinomycetes from antarctic sandstone rock samples:
RT   Micromonospora endolithica sp. nov. and two isolates related to
RT   Micromonospora coerulea Jensen 1932.";
RL   Syst. Appl. Microbiol. 27:166-174(2004).
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:RKN48644.1}.
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DR   EMBL; RBAK01000003; RKN48644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A9ZLM7; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000281726; 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, ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:RKN48644.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RKN48644.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000281726};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          35..180
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   DOMAIN          446..481
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   REGION          169..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          442..488
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   850 AA;  93778 MW;  C29482CD38EBDFB7 CRC64;
     MMGPGDFGSD PWDEFLARYF GRSEGGRRPA HRVDITRLMT ADAREMLADA ARRAAQRQSN
     DLDTDHLLWA ALQREPLRDL VRRAGADPDT LLNALGGRGD GAPRGEVPPN LSLTPAAKRA
     LLDAHQLSRA MGANYIGPEH ILMALPLNPE SPAGRMLAAG RIQPESLQAA NAERGSANGP
     RPDRGTPTLD QYGQDLTELA RMDQIDPVIG RADEIEQAVE ILSRRTKNNP VLIGEAGVGK
     TAIVEGLAER ICDGDVPQTL LGKRVIQLDL AGLVAGTRYR GDFEERLKKV IDEIRAHREE
     LIIFLDEIHT LVGAGGAGSE GGMDASNMLK PALARGELRV IGATTLDEYR RSIEKDAALA
     RRFQPVYVPE PTVEDTVAIL RGLRDRYEAH HQVRFTDEAL VAATELSDRY VTDRFLPDKA
     IDLIDQAGAR VRLRTRTPAS DVRELETQLD EVRRDKEQAV ADEQYEKASA LRDRLGELEE
     RIRHAQGNGD DSSRVPSVGP AEIAEVVSRA TGIPASQLTE EERDRLLRLE GHLHEKVVGQ
     DDAVTAVAEA VRRSRTGLAD PNRPMGSFLF LGPTGVGKTE LARALAEALF GEADRMVRVD
     MSEFQERHTV SRLVGAPPGY VGYEEAGQLT EAVRRRPYAV VLLDEIEKAH ADVFNVLLQV
     LDEGRLTDSQ GRTVNFKNTV LIMTSNLGSE LITGTQRAVG FGAGEGGGGE SDELRERLMR
     RLQENFRPEF LNRIDEVIIF RRLEAEQLRQ ITGLLLEETR RRMHAQDIQI EVTTAATDWL
     AEHGYQPEFG ARPLRRVIQR EVDNHLSRML LESAVSPGQK VTVDARDGGL TFDVSAGERD
     YSPATTSHPR
//
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