ID A0A4Y9PYM0_9MICO Unreviewed; 734 AA.
AC A0A4Y9PYM0;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=AAA family ATPase {ECO:0000313|EMBL:TFV84817.1};
GN ORFNames=E4V99_07175 {ECO:0000313|EMBL:TFV84817.1};
OS Microbacterium sp. dk485.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=2560021 {ECO:0000313|EMBL:TFV84817.1, ECO:0000313|Proteomes:UP000297593};
RN [1] {ECO:0000313|EMBL:TFV84817.1, ECO:0000313|Proteomes:UP000297593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=dk485 {ECO:0000313|Proteomes:UP000297593};
RA Dong K.;
RL Submitted (MAR-2019) 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:TFV84817.1}.
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DR EMBL; SPQW01000001; TFV84817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y9PYM0; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000297593; 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 CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 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; 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; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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, ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000297593};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 53..197
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 452..602
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 619..710
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 267..347
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 734 AA; 81282 MW; 3212FC100454113D CRC64;
MNATPQPGQE ESQSALEQFG INLTDRARQG KLDPVIGRDS EIRRVSQVLT RRTKNNPVLI
GEPGVGKTAV VEGLAQRIVA GDVAESLKDK ELVALDISAL VAGAMYRGQF EERLKSVLKE
ITESDGRVIT FIDELHVLMG AGGGEGSVAA SNMLKPMLAR GELRMIGATT LDEYREFIEK
DAALERRFQQ VYVGEPSVED TVAILRGLKE RYEAHHKVAI ADSALVAAAS LSNRYIPSRQ
LPDKAIDLID EAASRLRMEI DSAPLEIDEL RRHVDRLKLE ELALKKEKDD ASKERLAALR
ETLAGEQARL NELQARWERE RSSLNRVGDL KTRLDAARVE AERAQREGDL ERASRLLYAE
IPALERELMT AEREETEGER MVGDQVTEED IAEVIAAWTG IPVGKLMQGE TEKLLHLESE
LGKRLIGQKE AVKAVSDAIR RSRAGISDPH RPVGSFMFLG PTGVGKTELA KALAEFLFDD
EHAMVRIDMS EYGEKHSVSR LVGAPPGYVG YEQGGQLTEA VRRRPYSVVL LDEIEKAHPE
VFDVLLQVMD DGRLTDGQGR TVDFTNVILI LTSNLGSPIL IDPTLSAEQK REQVQALVRQ
AFKPEFINRL DDIVIFHVLS EDDLAQIVEL AVDALQRRLR ERRLTLAVTP DARAWLAERG
YDPVFGARPL RRLIQSEIQD RLAMAILAGR VRDGDVVRVD VAADGSSLVL TSDGAPTPPD
MSDDDEVIEA VLDD
//