ID A0A3G6ZIP6_9MICO Unreviewed; 736 AA.
AC A0A3G6ZIP6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=AAA family ATPase {ECO:0000313|EMBL:AZC12619.1};
GN ORFNames=DT073_01870 {ECO:0000313|EMBL:AZC12619.1};
OS Microbacterium sp. ABRD28.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=2268461 {ECO:0000313|EMBL:AZC12619.1, ECO:0000313|Proteomes:UP000280903};
RN [1] {ECO:0000313|EMBL:AZC12619.1, ECO:0000313|Proteomes:UP000280903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ABRD_28 {ECO:0000313|EMBL:AZC12619.1};
RA Jin H.M.;
RT "Genome sequence of Microbacterium sp. ABRD28.";
RL Submitted (JUL-2018) 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}.
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DR EMBL; CP031015; AZC12619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G6ZIP6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000280903; Chromosome.
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:UP000280903};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 53..197
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 452..595
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..374
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 736 AA; 81333 MW; 8A66A07821A387C1 CRC64;
MQATQMPGQE EQQSALEQFG INLTDRARQG KLDPVIGRDS EIRRVSQVLT RRTKNNPVLI
GESGVGKTAV VEGLAQRIVA GDVAESLKDK ELITLDISAL VAGAMYRGQF EERLKSVLKE
ITESEGRIIT FIDELHVLMG AGGGEGSVAA SNMLKPMLAR GELRLIGATT LNEYREFIEK
DAALERRFQQ VYVGEPSVED TVAILRGLKE RYEAHHKVAI SDGALVAAAS LSHRYIPSRQ
LPDKAIDLID EAASRLRMEI DSAPLEIDEL RRHVDRLKLE ELALKKEKDD ASRERLAVLR
DSLAGEQAKL DELQARWERE RSSLNKVGDL KTRLDAARIE AERAQREGNL EKASRILYAE
IPRLERDLVE AEREEPAGDR MVNDQVTEED IAAVIAAWTG IPVGRLMQGE TERLLHLEKE
LGKRIIGQRE AVRAVSDAVR RSRAGISDPN RPTGSFLFLG PTGVGKTELA KALAEFLFDD
EHAMVRIDMS EYGEKHSVSR LVGAPPGYIG YEQGGQLTEA VRRRPYSVVL LDEVEKAHPE
VFDVLLQVMD DGRLTDGQGR TVDFKNVIVI LTSNLGSPIL IDPTLSTEVK REQVQALVRQ
AFKPEFINRL DDIVIFQALT EDDLAQIVEL AVDLLQRRLK DRRLTLAVTP DARAWLAERG
YDPVFGARPL RRLIQSEIQD RLAMAILSGG VRDGDLVRVD VAADGSALVL TSDGPAAGSG
GGAAEEDEVI EAILED
//