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Database: UniProt
Entry: W3Y617_9FIRM
LinkDB: W3Y617_9FIRM
Original site: W3Y617_9FIRM 
ID   W3Y617_9FIRM            Unreviewed;       464 AA.
AC   W3Y617;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=ATP-dependent protease HslVU, ATPase subunit {ECO:0000313|EMBL:ETS93615.1};
GN   Name=hslU {ECO:0000313|EMBL:ETS93615.1};
GN   ORFNames=HMPREF1521_0348 {ECO:0000313|EMBL:ETS93615.1};
OS   Veillonella sp. AS16.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=936589 {ECO:0000313|EMBL:ETS93615.1, ECO:0000313|Proteomes:UP000019042};
RN   [1] {ECO:0000313|EMBL:ETS93615.1, ECO:0000313|Proteomes:UP000019042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS16 {ECO:0000313|EMBL:ETS93615.1,
RC   ECO:0000313|Proteomes:UP000019042};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JAN-2014) 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:ETS93615.1}.
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DR   EMBL; AZYX01000007; ETS93615.1; -; Genomic_DNA.
DR   RefSeq; WP_038115130.1; NZ_AZYX01000007.1.
DR   AlphaFoldDB; W3Y617; -.
DR   PATRIC; fig|936589.3.peg.363; -.
DR   eggNOG; COG1220; Bacteria.
DR   Proteomes; UP000019042; Unassembled WGS sequence.
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:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Hydrolase {ECO:0000313|EMBL:ETS93615.1};
KW   Protease {ECO:0000313|EMBL:ETS93615.1}.
FT   DOMAIN          50..353
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          356..450
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
SQ   SEQUENCE   464 AA;  52272 MW;  467D801B45F27FA9 CRC64;
     MKDNYTPKQI VAELDKYIIG QKEAKKMVAI ALRNRWRAKQ LPEEVRDEYV PKNILLIGPT
     GVGKTELARR LAKIMHAPFV KVEATKYTEV GYVGRDVESM VRDLLLNSIR MVKEDKKTKN
     HVKATRLANQ RLVDILLPSS GGAKKFTNPL EMLFNNNEEK SESKADIKTE SKADERETLL
     KQISGGLLDD KEITIEVRDQ QKNVAGIGAG TSQEDMANNI QDMLNAMMPK RTKKRTTTVK
     NARTIFAEEI AEDMLDMDEV HEEAIKLAER EGIIFIDEFD KIAAGNENVR GVVSREGVQR
     DILPIVEGSM VSTKFGPVNT EHILFIAAGA FHVSKPSDLI PELQGRFPIR VELNSLSKED
     FKAILTTPQQ ALLKQYYMLL QADNVTVHFT DESIDKIAEL AYRVNNETED IGARRLHTIL
     ENLLQDVSYN APAPEPVEVT ITAAMVEDRL NTLVEDQDLS QYIL
//
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