ID A0A0Q8LZE6_9MICO Unreviewed; 861 AA.
AC A0A0Q8LZE6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=AAA family ATPase {ECO:0000313|EMBL:KRB38996.1};
GN ORFNames=ASD93_03435 {ECO:0000313|EMBL:KRB38996.1};
OS Microbacterium sp. Root180.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736483 {ECO:0000313|EMBL:KRB38996.1, ECO:0000313|Proteomes:UP000050802};
RN [1] {ECO:0000313|EMBL:KRB38996.1, ECO:0000313|Proteomes:UP000050802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root180 {ECO:0000313|EMBL:KRB38996.1,
RC ECO:0000313|Proteomes:UP000050802};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB38996.1, ECO:0000313|Proteomes:UP000050802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root180 {ECO:0000313|EMBL:KRB38996.1,
RC ECO:0000313|Proteomes:UP000050802};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KRB38996.1}.
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DR EMBL; LMHS01000001; KRB38996.1; -; Genomic_DNA.
DR RefSeq; WP_056118571.1; NZ_LMHS01000001.1.
DR AlphaFoldDB; A0A0Q8LZE6; -.
DR STRING; 1736483.ASD93_03435; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000050802; Unassembled WGS sequence.
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; -; 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 78, MITOCHONDRIAL; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000050802};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 39..182
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 455..490
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
SQ SEQUENCE 861 AA; 92590 MW; 03F763C9C07CB5CE CRC64;
MPEDFTPSTG ADDSERSFDE FLARYLAGER TRAQRSIDLS RFLGARTQEL LQRAGRFALE
RGQRELDALH VLRVLVEEPP ARDAVEHIGA DPRAILRAAE ERLPAASAPA DVDGAVITSS
VQRALFHAFQ VARSSGSTYV DPEHLFFALV LAQDTPAGQV LARAGVTAEA LTQGLRETVT
PSRATDTEEG TDAAASDTPM LDTYGTDLTA RAADGDLDPV IGRADEIEQT IEILSRRTKN
NPVLVGEAGV GKTAIVEGLA QAIVDGAVPE QLLGKRVISL DLPAMLAGTR YRGDFEERLT
KTMDEISARK DELVIFLDEV HTVVGAGGAG DGGMDAGNIL KPRLARGDLH LVGATTLKEY
RAIEKDPALE RRFQPVRVGE PGIEDAVLIL HGLKPAYEEH HGIVYTDEAI RAAVELSDRY
LSERVLPDKA IDLIDQAGAR LRLRLGAKVD VTGLVEQLAT LEADKNAAVT AEHYEEASRL
RDQLSAVQAR LDDVTASGAA ARGEAVVGEP EIAAVISRAT GIPVNRLTEP ERERLAQLDD
ELHDRVIGQD DAVAAVAKAV RRNRTGMGDA RRPVGSFLFL GPTGVGKTEL AKALAASLFP
SGSGQGGGEG SVIRFDMSEF GERHTVSRLV GAPPGYVGYE EAGQLTERVR RNPYSIVLFD
EIEKAHPDVF NLLLQVLDDG RLTDGQGRTV DFRNTVVVMT SNLGSEFLAS RGGAIGFLAD
GGGPTGYGSE KDLRDRVFAK LREAMRPEFL NRIDEIVLFR KLDKPQLRQI VGLLLGASEA
RLAKREVALV VTDAAIDWLA DNGYEPEYGA RPLRRLIQRE VDDRVADLFV TGALVDGGTV
TVDAAPDGLT VRAGVALTVA A
//
