ID D6RXK8_BORVA Unreviewed; 755 AA.
AC D6RXK8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=ATP-dependent Clp protease, subunit A {ECO:0000313|EMBL:EEF81761.1};
GN ORFNames=BVAVS116_0365 {ECO:0000313|EMBL:EEF81761.1};
OS Borreliella valaisiana VS116.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=445987 {ECO:0000313|EMBL:EEF81761.1, ECO:0000313|Proteomes:UP000006163};
RN [1] {ECO:0000313|EMBL:EEF81761.1, ECO:0000313|Proteomes:UP000006163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS116 {ECO:0000313|EMBL:EEF81761.1,
RC ECO:0000313|Proteomes:UP000006163};
RA Fraser-Liggett C.M., Mongodin E.F., Casjens B., Dunn J., Luft B., Qiu W.,
RA Schutzer S., Sebastian Y.;
RL Submitted (JAN-2009) 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}.
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:EEF81761.1}.
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DR EMBL; ABCY02000001; EEF81761.1; -; Genomic_DNA.
DR AlphaFoldDB; D6RXK8; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_12; -.
DR Proteomes; UP000006163; Unassembled WGS sequence.
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 Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR018368; ClpA/B_CS1.
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 78, MITOCHONDRIAL; 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 SMART; SM00382; AAA; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00870; CLPAB_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Hydrolase {ECO:0000313|EMBL:EEF81761.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:EEF81761.1}.
FT DOMAIN 221..366
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 755 AA; 87680 MW; BF8C7D40DDC62F51 CRC64;
MFFNTFLFFM ESKHLVFTEE HIFYGLIKSD KVKELLSLCT IDFDKLNKQL EEFFSKLPLR
DNYIPDYVSS MDYLYDDIIG VLFFYKKPYK IQEKDLLWVL VKKRKNSILD ALVNSGFNLT
IFDKLIEVHD YLAANTKSDS GYGSELIAEY IHNNAPKSKG GFHIFEDNRD KLDKNNIFLE
NKDSIGNFLT NVIDTLNVKY NPLIGRKREL SRLIQVILRK HKSNPILFGE PGVGKTVLIQ
GLAYKIKIEN VPVDLIGYEI YSLDIGRLVS GTKYRGDLES RINRVLDFLN SRKKVILFID
EIHMIVGAGA TSFGSMDISN LLKPILTLGK IKFIGATTEY EYRKFFLKDK ALIRRFQSIE
LKEPNFDDTY IILQEIKKDY ERYHNVEYTD EAIQACIVMS QKYIKDRFLP DKAFDILDEL
GSKFKLENIK RTITKDDVCD LIKSFVGSNI FNFEEYDSEL LINLENRIKK ELIIEDSLVF
DLMLNIKLLK FNLLTNRSTI GLFAFIGASG AGKCKLTDIL SEEFKIPKFS LNMSEYSDFN
ALDRLIGPVL SNEGYYESTR FFKFLNKSSN SIIFLSDFDK CNKRVLDFFL EGFKTGKLFD
GLGKKVSLSE SLIVISVNTE GNELNSIGFK NKIAEGNDVN FILKKRFPNE FLDLIDHVFV
FKSIDELDFE KIILNELNSF AKILKDRKFD IFFEKSVVDY IREKIYGKGY GLKSVKKFIF
KEVGKLLIDE ILFKKIENFG KIKIYLDETI KYEFL
//
