ID A0A4V0YD41_9MICO Unreviewed; 732 AA.
AC A0A4V0YD41;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=AAA family ATPase {ECO:0000313|EMBL:QAY59391.1};
GN ORFNames=ET475_04880 {ECO:0000313|EMBL:QAY59391.1};
OS Microbacterium protaetiae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=2509458 {ECO:0000313|EMBL:QAY59391.1, ECO:0000313|Proteomes:UP000293995};
RN [1] {ECO:0000313|EMBL:QAY59391.1, ECO:0000313|Proteomes:UP000293995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DFW100M-13 {ECO:0000313|EMBL:QAY59391.1,
RC ECO:0000313|Proteomes:UP000293995};
RA Heo J., Kim S.-J., Kim J.-S., Hong S.-B., Kwon S.-W.;
RT "Genome sequencing of strain DFW100M-13.";
RL Submitted (JAN-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}.
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DR EMBL; CP035494; QAY59391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V0YD41; -.
DR KEGG; mprt:ET475_04880; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000293995; 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:UP000293995};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 53..197
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 454..603
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 621..712
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 267..374
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 732 AA; 81000 MW; 1E25AFA901804D4F CRC64;
MNAQPQPGQE EQQSPLEQFG INLTDRARQG KLDPVIGRDS EIRRVSQVLT RRTKNNPVLI
GEPGVGKTAV VEGLAQRIVA GDVAESLKDK ELIALDISAL VAGAMYRGQF EERLKSVLKE
ITESEGRVIT FIDELHVLMG AGGGEGSVAA SNMLKPMLAR GELRLIGATT LDEYREFVEK
DAALERRFQQ VYVGEPSVED TIAILRGLKG RYEAHHGVTI SDSALVAAAA MSNRYIPSRQ
LPDKAIDLID EAMSRLKMEI DSSPVEIDQL KRAVDRMRLE ELALKKEKDD ASKERLAKLR
EQMAESEKEL SGLEARWERE RAGLNRVGEL KKQLDQATTD RDRALREADY AKASRLEYET
IKKLQQQLAE AEQAEAQPAE PRMVNEQVTD DDIAAVIASW TGIPVGRLLQ GETEKLLHLE
SELGKRLIGQ KEAVKAVSDA VRRSRAGISD PNRPTGSFLF LGPTGVGKTE LAKALAEFLF
DDEHAMVRID MSEYGEKHSV SRLVGAPPGY IGYEQGGQLT EAVRRRPYSV VLLDEVEKAH
PEVFDVLLQV LDDGRLTDGQ GRTVDFKNVI LILTSNIGSP ILIDPMLTTA QKREQVMGLV
RSSFRPEFLN RLDDIVMFQA LTEDDLAQIV ELSVDQLQQR LHERRLTLAV TPDARAWLAR
RGYDPVFGAR PLRRLIQSEI QDRLAMAILG GTVHDGDVVR VDVAADDSSL VLTSDGPATG
PDDDVIEAEL VD
//