ID A0A2A9M8Y6_9APIC Unreviewed; 1039 AA.
AC A0A2A9M8Y6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE SubName: Full=Putative ATP-dependent hsl protease ATP-binding subunit hslU {ECO:0000313|EMBL:PFH32087.1};
GN ORFNames=BESB_020280 {ECO:0000313|EMBL:PFH32087.1};
OS Besnoitia besnoiti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH32087.1, ECO:0000313|Proteomes:UP000224006};
RN [1] {ECO:0000313|EMBL:PFH32087.1, ECO:0000313|Proteomes:UP000224006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH32087.1,
RC ECO:0000313|Proteomes:UP000224006};
RA Schares G., Venepally P., Lorenzi H.A.;
RT "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000256|ARBA:ARBA00009771}.
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:PFH32087.1}.
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DR EMBL; NWUJ01000012; PFH32087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9M8Y6; -.
DR STRING; 94643.A0A2A9M8Y6; -.
DR VEuPathDB; ToxoDB:BESB_020280; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000224006; Chromosome xi.
DR GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
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 Gene3D; 1.10.8.60; -; 1.
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; IPR004491; HslU.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00390; hslU; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR48102:SF3; ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:PFH32087.1};
KW Hydrolase {ECO:0000313|EMBL:PFH32087.1};
KW Nucleotide-binding {ECO:0000313|EMBL:PFH32087.1};
KW Protease {ECO:0000313|EMBL:PFH32087.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000224006}.
FT DOMAIN 637..931
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 930..1025
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..522
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..570
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1039 AA; 109289 MW; 7EA60EDCF568250F CRC64;
MWRVAAYAAG HSPPGSSGGL RRQSARQAYS SSAGNPTSFS FSKRCSSPSC TTGESRNRGE
QTGGRRCFRP GAGSPAPHHS DSFAARSASS SLPSSAPSSP RASLESLRAS FPPPLPGSCC
SADAGTRRVC LSALSSPRLS PLSQPVALSF APRRSAGGSS SAFSLFSKRS VSFGAHAQNQ
PASHARVSFL LSRLSGSPVP CPSAKRFLSH SASDGDGRSE DPRQAIDGDP ARNSPPRPPC
GAPSIEAVGG VRTPEPGSDG EARAHSGCGS FSLRGPKTGA SCRQAERGGM MSYGTLEGGR
SGEKVRDSGS RQGESCSQQG RAAAEPDASS SPLLRAPRVP PGSGRPAPSA LSARRPQAAE
GSQRTSASSS SASSFPPLGE RARANAVASA ERSRVPSPLF DSSGGSAKAL GGGAPCAQPE
PWPPAPPAPV SAFPDAGTDS PFFSPPCAAA SLRLPAAPAS PAVLALPQVS LAPRNGPFRG
ASAPPAPSAE PDCPLSSPPP SSALPPSSAL PPSSPWPPQF SPFSPSRVAS FSAAPPPASS
LSSPGSASPA PPPPSSGPAS LSPPPPRCPA AEQGAGGSSL AVEAATKSQA LCPSEMVAYL
DKYIVGQADA KKAVAVALRQ RWRRRQIEDE KLRDDITPKN ILLIGPTGVG KTEVARRLAR
CIDAPFIKVE ATKFTEVGFH GRDVDQIIKD LVEVAMKNQR TRLQEAMRPT AERRAETKIL
EALLGQMPAE EHQQWLEHLR GGALDSRRVH VDIPPARQHG APPGVAGFDE SGRDSIVADL
ESIIRDIDRP RHAFFTARRG ARGLEARNLT VKEARKKLMQ AELDAMITKD LVVQKALEAV
EQEGIVFIDE IDKICTKGGR SGYNPDASDE GVQRDLLPLI EGTTVTTRYG DVRTDYILFI
ASGAFHCVRP SDLLAELQGR LPIRVTLKPL AEADLRDILT KTKNNLIEQN RALLQTEKVD
LHFTEEAVNE IARVACEVNA NVENIGARRL HTIIEKIMED VNFAAPSMAP GMRVEIDLER
VRSSVSSLLT KMDYTRFVL
//