ID A0A0M3V1W1_CAMC5 Unreviewed; 440 AA.
AC A0A0M3V1W1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Heat shock protein HslVU, ATPase subunit {ECO:0000313|EMBL:ALF45125.1};
DE EC=3.4.25.2 {ECO:0000313|EMBL:ALF45125.1};
GN Name=hslU {ECO:0000313|EMBL:ALF45125.1};
GN ORFNames=CCV52592_1973 {ECO:0000313|EMBL:ALF45125.1};
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105 {ECO:0000313|EMBL:ALF45125.1, ECO:0000313|Proteomes:UP000006380};
RN [1] {ECO:0000313|Proteomes:UP000006380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92 {ECO:0000313|Proteomes:UP000006380};
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000256|ARBA:ARBA00009771}.
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DR EMBL; CP000767; ALF45125.1; -; Genomic_DNA.
DR RefSeq; WP_041743300.1; NC_009715.2.
DR AlphaFoldDB; A0A0M3V1W1; -.
DR STRING; 360105.CCV52592_1973; -.
DR KEGG; ccv:CCV52592_1973; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000006380; Chromosome.
DR GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR CDD; cd19498; RecA-like_HslU; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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 Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:ALF45125.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006380};
KW Stress response {ECO:0000313|EMBL:ALF45125.1}.
FT DOMAIN 48..329
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 332..426
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 207..238
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 440 AA; 49463 MW; 81026AF810835C1C CRC64;
MNMTPKQIVE FLDDYVIGQK DAKKIIAIAL RNRYRRMKLE KAIQDDIMPK NILMIGSTGV
GKTEIARRLS KMMGMPFIKV EASKYTEVGF VGRDVESMVR DLAMAAFNLV KAEQSEKNQD
KINAYIEEKI VSKLLPPLPK GASEEKTADY ERSYEKMLAK FRNGDLDDLT VEIEIQQNSL
ETGSNVPPDM AQMQESFIKI IGMGSKNVKK EMKVKDAKKA LENEANDKIL DIESIKTQAI
RRAENEGIIF IDEIDKVAVS SAGSSRQDPS KEGVQRDLLP IVEGSNVSTK FGNLKTDHIL
FIAAGAFHIS KPSDLIPELQ GRFPLRVELD SLDEKALYQI LTKPKNSLLK QYIALLSTEN
VELAFDDEAI HEIAKIAQAA NEKMEDIGAR RLHTVIERVI EDISFEASEK SGEKVNVTKE
LVKERLSDVV EDQDLARYIL
//