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
//